P. Balaram

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Enhancing peptide antigenicity by helix stabilization

R. Gurunath, T. K. Beena, P. Adiga, 1995, FEBS letters.

Beta-hairpins in proteins revisited: lessons for de novo design.

K. Gunasekaran, C. Ramakrishnan, P. Balaram, 1997, Protein engineering.

Orthogonal beta beta motifs in proteins.

R. Sowdhamini, C. Ramakrishnan, N. Srinivasan, 1992, Journal of molecular biology.

Conformations of disulfide bridges in proteins.

R. Sowdhamini, C. Ramakrishnan, N. Srinivasan, 2009, International journal of peptide and protein research.

Characterization of contryphans from Conus loroisii and Conus amadis that target calcium channels

P. Balaram, V. Sabareesh, K. H. Gowd, 2006, Peptides.

Rapid mass spectral identification of contryphans. Detection of characteristic peptide ions by fragmentation of intact disulfide-bonded peptides in crude venom.

P. Balaram, S. Thakur, 2007, Rapid communications in mass spectrometry : RCM.

Asymmetric Total Synthesis of Erythromycin. 1. Synthesis of an Erythronolide A Seco Acid Derivative via Asymmetric Induction

K. Nambiar, E. Logusch, P. Balaram, 1981 .

Asymmetric total synthesis of erythromycin. 2. Synthesis of an erythronolide A lactone system

P. Balaram, L. Browne, C. H. Chen, 1981 .

Asymmetric total synthesis of erythromycin. 3. Total synthesis of erythromycin

K. Nambiar, E. Logusch, P. Balaram, 1981 .

Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design.

H. Balaram, S. Ray, P. Balaram, 1997, Structure.

Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state.

S. Parthasarathy, M. Murthy, H. Balaram, 2002, Biochemistry.

Vibrational Circular Dichroism of -Hairpin Peptides

P. Balaram, C. Das, Chunxia Zhao, 2000 .

Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis.

N Srinivasan, R Sowdhamini, B Shoichet, 1989, Protein engineering.

A designed three-stranded β-sheet in an α/β hybrid peptide.

P. Balaram, R. Sonti, H. Gopi, 2013, Chemistry.

NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded β-sheet peptide.

P. Balaram, R. Sonti, S. Ragothama, 2012, Journal of Physical Chemistry B.

X-Ray crystal structure of pivaloyl-D-Pro-L-Pro-L-Ala-N-methylamide; observation of a consecutive β-turn conformation

M. Vijayan, P. Balaram, C. M. Nair, 1979 .

Tandem electrospray mass spectrometric studies of proton and sodium ion adducts of neutral peptides with modified N- and C-termini: synthetic model peptides and microheterogeneous peptaibol antibiotics.

P. Balaram, V. Sabareesh, 2006, Rapid communications in mass spectrometry : RCM.

Structural characteristics of alpha-helical peptide molecules containing Aib residues.

I. Karle, P. Balaram, P Balaram, 1990, Biochemistry.

Subunit interface mutation disrupting an aromatic cluster in Plasmodium falciparum triosephosphate isomerase: effect on dimer stability.

Hemalatha Balaram, H. Balaram, P. Balaram, 2002, Protein engineering.

Thermal stabilization of thymidylate synthase by engineering two disulfide bridges across the dimer interface.

D. Santi, P. Balaram, S. Agarwalla, 1994, Journal of molecular biology.

Negative nuclear Overhauser effects as probes of macromolecular structure.

J. Dadok, P. Balaram, A. Bothner-By, 1972, Journal of the American Chemical Society.

Localization of tyrosine at the binding site of neurophysin II by negative nuclear Overhouser effects

P. Balaram, E. Breslow, A. Bothner-By, 1972 .

Stereochemical punctuation marks in protein structures: glycine and proline containing helix stop signals.

H. A. Nagarajaram, C. Ramakrishnan, P. Balaram, 1998, Journal of molecular biology.

A STUDY ON THE DOMINATING TRANSVERSAL CHROMATIC NUMBER

P. Balaram, P. Sujatha, 2015 .

Ionophore-mediated transmembrane movement of divalent cations in small unilamellar liposomes: An evaluation of the chlortetracycline fluorescence technique and correlations with black lipid membrane studies

P. Balaram, R. Nagaraj, M. Mathew, 2005, The Journal of Membrane Biology.

A highly active chemotactic peptide analog incorporating the unusual residue 1-aminocyclohexanecarboxylic acid at position 2.

P. Balaram, E. Becker, M. Sukumar, 1985, Biochemical and biophysical research communications.

Cystine peptides: The intramolecular antiparallel β‐sheet conformation of a 20‐membered cyclic peptide disulfide

P. Balaram, R. Kishore, S. Raghothama, 1987, Biopolymers.

Conformational effects on peptide aggregation in organic solvents: Spectroscopic studies of two chemotactic tripeptide analogs

P. Balaram, P. Raj, 1985, Biopolymers.

Circular dichroism studies of α‐aminoisobutyric acid‐containing peptides: Chain length and solvent effects in alternating Aib‐L‐Ala and Aib‐L‐Val sequences

P. Balaram, E. K. Vijayakumar, T. Sudha, 1984 .

An internally quenched fluorescent substrate for collagenase

P. Balaram, Y. K. Saikumari, P. Balaram, 2008, Biopolymers.

Helical peptide models for protein glycation: proximity effects in catalysis of the Amadori rearrangement.

P. Balaram, J. Venkatraman, K. Aggarwal, 2001, Chemistry & biology.

Design and construction of an open multistranded beta-sheet polypeptide stabilized by a disulfide bridge.

P. Balaram, G. A. Nagana Gowda, J. Venkatraman, 2002, Journal of the American Chemical Society.

Structural effects on the formation of proton and alkali metal ion adducts of apolar, neutral peptides: electrospray ionization mass spectrometry and Ab initio theoretical studies.

J. Chandrasekhar, P. Balaram, M. Panda, 2002, Chemistry.

Transcriptomic profiling of the medicinal plant Clitoria ternatea: identification of potential genes in cyclotide biosynthesis

R. Sowdhamini, P. Balaram, R. Venkatesan, 2020, Scientific Reports.

Conformationally restricted formyl methionyl tripeptide chemoattractants: a three-dimensional structure-activity study of analogs incorporating a C alpha,alpha-dialkylated glycine at position 2.

C. Toniolo, M. Crisma, P. Balaram, 1989, Peptide research.

Crystal Structures of a New Polymorphic Form of Gabapentin Monohydrate and the E and Z Isomers of 4‐Tertiarybutylgabapentin

P. Balaram, S. Aravinda, K. Nagarajan, 2009, Chemical biology & drug design.

Proteolytic stability of β‐peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site

H. Balaram, P. Balaram, P. Pattanaik, 2003, FEBS letters.

Structure formation in short designed peptides probed by proteolytic cleavage.

P. Balaram, G. Ravindra, Y. K. Saikumari, 2006, Protein and peptide letters.

Identification and characterization of a library of microheterogeneous cyclohexadepsipeptides from the fungus Isaria.

H. Balaram, P. Balaram, V. Sabareesh, 2007, Journal of natural products.

Two Novel Hexadepsipeptides with Several Modified Amino Acid Residues Isolated from the Fungus Isaria

I. Karle, P. Balaram, G. Ravindra, 2004, Chemistry & biodiversity.

DETERMINATION OF $-TURN CONFORMATION BY LASER RAMAN SPECTROSCOPY

A. Tu, P. Balaram, R. Nagaraj, 2005 .

Aib Residues in Peptaibiotics and Synthetic Sequences: Analysis of Nonhelical Conformations

P. Balaram, S. Aravinda, N. Shamala, 2008, Chemistry & biodiversity.

The properties of ion channels formed by zervamicins

M. Sansom, P. Balaram, I. Mellor, 2004, European Biophysics Journal.

Zervamicins, a structurally characterised peptide model for membrane ion channels.

J. Flippen-Anderson, I. Karle, M. Sansom, 1992, Biochemical and biophysical research communications.

Possible Ion Channel Model in Crystals of Leu-Zervamicin,

J. Flippen-Anderson, I. Karle, P. Balaram, 1992 .

Mass spectrometric analysis of dimer-disrupting mutations in Plasmodium triosephosphate isomerase.

D. Bandyopadhyay, P. Balaram, Kallol Gupta, 2016, Analytical biochemistry.

Identification of α- and β-hydroxy acid containing cyclodepsipeptides in natural peptide mixtures using negative ion mass spectrometry

P. Balaram, S. Thakur, Kallol Gupta, 2009, Journal of the American Society for Mass Spectrometry.

Rapid mass spectrometric determination of disulfide connectivity in peptides and proteins.

Moitrayee Bhattacharyya, P. Balaram, Kallol Gupta, 2013, Molecular bioSystems.

Structure of triosephosphate isomerase (TIM) from Methanocaldococcus jannaschii.

M. Murthy, P. Gayathri, H. Balaram, 2007, Acta crystallographica. Section D, Biological crystallography.

Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase

H. Balaram, P. Balaram, M. Banerjee, 2009, The FEBS journal.

Characterization of the interaction of lipid A and lipopolysaccharide with human serum albumin: implications for an endotoxin carrier function for albumin

P. Balaram, V. Mathan, S. David, 1995 .

Stabilization of beta-turn conformations in enkephalins. alpha-Aminoisobutyric acid analogs.

P. Balaram, T. Sudha, 1983, International journal of peptide and protein research.

Homologous cholinergic fluorescent probes. Synthesis and fluorescence properties

P. Balaram, R. Narayanan, 1978, FEBS letters.

Quantitation and characterization of glutathionyl haemoglobin as an oxidative stress marker in chronic renal failure by mass spectrometry.

P. Balaram, A. Mandal, A. Rao, 2007, Clinical biochemistry.

The fully‐extended conformation in peptides and proteins

C. Alemán, C. Toniolo, F. Formaggio, 2018 .

Conformations of β‐amino acid residues in peptides: X‐ray diffraction studies of peptides containing the achiral residue 1‐aminocyclohexaneacetic acid, β3,3Ac6c

P. Balaram, R. Rai, N. Shamala, 2008, Biopolymers.

Fragmentation of peptide disulfides under conditions of negative ion mass spectrometry: Studies of oxidized glutathione and contryphan

P. Balaram, S. Thakur, 2008, Journal of the American Society for Mass Spectrometry.

Novel Peptides of Therapeutic Promise from Indian Conidae

M. Ramaswami, S. Sikdar, P. Iengar, 2005, Annals of the New York Academy of Sciences.

Novel Peptides of Therapeutic Promise from Indian

M. Ramaswami, S. Sikdar, P. Iengar, 2005 .

Sodium channel modulating activity in a delta-conotoxin from an Indian marine snail.

M. Ramaswami, A. K. Lala, S. Sikdar, 2003, FEBS letters.

Revisiting the burden borne by fumarase: enzymatic hydration of an olefin

H. Balaram, P. Balaram, S. Balasubramanian, 2022, bioRxiv.

Bull sperm plasma and acrosomal membranes: fluorescence studies of lipid phase fluidity.

P. Balaram, S. Vijayasarathy, S. Shivaji, 1982, Biochemical and biophysical research communications.

Characterization of the interactions of a polycationic, amphiphilic, terminally branched oligopeptide with lipid A and lipopolysaccharide from the deep rough mutant of Salmonella minnesota

S. Awasthi, P. Balaram, B. Lindner, 1996 .

Synthetic and conformational studies on dehydrophenylalanine containing model peptides

Virander S. Chauhan, P. Balaram, K. Uma, 2009 .

Conformations of dehydrophenylalanine containing peptides. NMR studies on three tripeptides with a central dehydrophenylalanyl residue.

Virander S. Chauhan, P. Balaram, A. Sharma, 2009 .

Cystine peptides. Spectroscopic studies on the conformations of a cyclic pentapeptide disulfide

P. Balaram, R. Kishore, S. Raghothama, 2009 .

Characterization of folded conformations in a tetrapeptide containing two tryptophan residues by vibrational circular dichroism.

Ana G. Petrovic, P. Balaram, P. Polavarapu, 2009, Chirality.

Conformations of dehydrophenylalanine containing peptides. Nuclear Overhauser effect study of two acyclic tetrapeptides.

Virander S. Chauhan, P. Balaram, A. Kumar, 2009, International journal of peptide and protein research.

Nuclear Overhauser Effects and circular Dichroism as Probes of \beta.-turn Conformations in Acyclic and Cyclic Peptides with Pro-X Sequences

H. Balaram, P. Balaram, Anilesh Kumar, 1983 .

1H N.M.R. studies of protected alpha-aminoisobutyric acid containing peptides. Chemical shift nonequivalence of benzyloxycarbonyl methylene protons.

P. Balaram, R. Nagaraj, M. Iqbal, 2009, International journal of peptide and protein research.

X‐Pro peptides: Solution and solid‐state conformation of benzyloxycarbonyl‐(Aib‐Pro)2methyl ester, a type I β‐turn

M. Vijayan, P. Balaram, C. M. Nair, 1981 .

Conformational analysis of an active chemotactic peptide analog containing z-dehydrophbnylalanine at position 3

Virander S. Chauhan, P. Balaram, K. Uma, 1988 .

ProtonNMR studies of peptide conformations

P. Balaram, 1985, Proceedings / Indian Academy of Sciences.

Peptide models for beta-turns. A circular dichroism study.

M. Crisma, H. Balaram, P. Balaram, 1984, International journal of peptide and protein research.

13C NMR studies on trifluoroacetyl derivatives of 2‐acetamido‐2‐deoxyhexoses

P. Balaram, M. Ranganathan, 1984 .

Trifluoroacetic anhydride. A convenient NMR solvent for carbohydrates. 270 MHz 1H NMR studies of 2‐acetamido‐2‐deoxyhexoses

P. Balaram, M. Ranganathan, 1980 .

Synthesis of homologous fluorescent carboxylates and their application to the study of bovine serum albumin

P. Balaram, R. Narayanan, 1980 .

Unmasking of tyrosyl fluorescence in serum albumins on bilirubin binding

P. Balaram, M. Mathew, M. Mathew, 1980, FEBS letters.

Structural chemistry of peptides containing backbone expanded amino acid residues: conformational features of β, γ, and hybrid peptides.

P. Balaram, Sunanda Chatterjee, N. Shamala, 2011, Chemical reviews.

Differences in hydration and association of helical Boc-Val-Ala-Leu-Aib-Val-Ala-Leu-(Val-Ala-Leu-Aib)2-OMe.xH2O in two crystalline polymorphs.

J. Flippen-Anderson, I. Karle, P. Balaram, 1992, Journal of medicinal chemistry.

13C nuclear magnetic resonance studies of the binding of alkali and alkaline earth metal salts to amides

C. Rao, P. Balaram, C. Rao, 1980 .

Characterization of alkali induced formation of lanthionine, trisulfides, and tetrasulfides from peptide disulfides using negative ion mass spectrometry

P. Balaram, S. Thakur, 2009, Journal of the American Society for Mass Spectrometry.

Fluorescent alamethicin fragments. A study of membrane activity and aqueous phase aggregation.

P. Balaram, R. Nagaraj, M. Mathew, 1981, Biochimica et biophysica acta.

Alamethicin and synthetic peptide fragments as uncouplers of mitochondrial oxidative phosphorylation. Effect of chain length and charge.

P. Balaram, R. Nagaraj, M. Mathew, 1981, Biochemical and Biophysical Research Communications - BBRC.

Plasma membrane bound Ca2+‐ATPase activity in bull sperm

P. Balaram, S. Vijayasarathy, S. Shivaji, 1980, FEBS letters.

Interaction of melittin with endotoxic lipid A.

P. Balaram, V. Mathan, S. Alwin David, 1992, Biochimica et biophysica acta.

The murky origins of the coronavirus SARS-CoV-2, the causative agent of the COVID-19 pandemic

P. Balaram, 2021 .

Synthetic peptides as chemoattractants for bull spermatozoa structure activity correlations.

P. Balaram, M. Iqbal, S. Vijayasarathy, 1980, Biochemical and biophysical research communications.

An electrospray ionization mass spectrometry investigation of 1-anilino-8-naphthalene-sulfonate (ANS) binding to proteins

S. Ray, P. Balaram, S. Singh, 2001, Journal of the American Society for Mass Spectrometry.

Circular Dichroism of Designed Peptide Helices and β‐Hairpins: Analysis of Trp‐ and Tyr‐Rich Peptides

P. Balaram, P. Polavarapu, R. Mahalakshmi, 2005, Chembiochem : a European journal of chemical biology.

Alamethicin, a Transmembrane Channel

P. Balaram, R. Nagaraj, 1981 .

1-Anilino-8-naphthalene-sulfonate (ANS) Binding to Proteins Investigated by Electrospray Ionization Mass Spectrometry: Correlation of Gas-Phase Dye Binding to Population of Molten Globule States in Solution

S. Ray, P. Balaram, 1999 .

Nuclear magnetic resonance studies of the interaction of peptides and hormones with bovine neurophysin.

P. Balaram, E. Breslow, A. Bothner‐By, 1973, Biochemistry.

Effects of hydrogen-bond deletion on peptide helices: structural characterization of depsipeptides containing lactic acid.

I. Karle, P. Balaram, C. Das, 2001, Biopolymers.

Alpha-gamma hybrid peptides that contain the conformationally constrained gabapentin residue: characterization of mimetics of chain reversals.

P. Balaram, S. Aravinda, N. Shamala, 2003, Chemistry.

Non-standard amino acids in peptide design and protein engineering

P. Balaram, Padmanabhan Balaram, 1992, Current Biology.

Design of folded peptides.

P. Balaram, S. C. Shankaramma, J Venkatraman, 2001, Chemical reviews.

Stereochemically constrained peptides. Theoretical and experimental studies on the conformations of peptides containing 1-aminocyclohexanecarboxylic acid

Claudio Toniolo, C. Toniolo, P. Balaram, 1986 .

Peptide-lanthanide interactions. Crystal structure of a europium(III)-triglycine complex.

P. Balaram, M. Nethaji, S. S. Krishnamurthy, 2009, International journal of peptide and protein research.

The Structural Characterization of Folded Peptides Containing the Conformationally Constrained beta-Amino Acid Residue beta(2,2)Ac(6)c

P. Balaram, N. Shamala, K. Basuroy, 2012 .

Conformations of peptides containing Z-alpha,beta-dehydroleucine (delta ZLeu). A comparison of Boc-Pro-delta ZLeu-Gly-NHEt and Boc-Pro-delta ZPhe-Gly-NHEt.

Virander S. Chauhan, P. Balaram, A. Sharma, 1989, International journal of biological macromolecules.

Conformations of dehydrophenylalanine containing peptides: nmr studies of an acyclic hexapeptide with two Δz‐Phe residues

Virander S. Chauhan, P. Balaram, K. Uma, 1989, Biopolymers.

An incipient 310 helix in Piv-Pro-Pro-Ala-NHMe as a model for peptide folding

P. Balaram, Y. Venkatachalapathi, 1979, Nature.

Stereochemically constrained linear peptides. Conformations of peptides containing .alpha.-aminoisobutyric acid

P. Balaram, R. Nagaraj, N. Shamala, 1979 .

Stereochemical Analysis of Higher α,α-Dialkylglycine Containing Peptides. Characterization of Local Helical Conformations at Dipropylglycine Residues and Observation of a Novel Hydrated Multiple β-Turn Structure in Crystals of a Glycine Rich Peptide

I. Karle, P. Balaram, S. Raghothama, 1997 .

Cyclic cystine peptides. Antiparallel β-sheet conformation for the 20-membered ring in Boc-Cys-Val-Aib-Ala-Leu-Cys-NHMe

I. Karle, P. Balaram, R. Kishore, 1988 .

Stereochemical control of peptide folding.

P. Balaram, R. Kaul, 1999, Bioorganic & medicinal chemistry.

Contrasting solution conformations of peptides containing α,α‐dialkylated residues with linear and cyclic side chains

P. Balaram, R. Rao, S. Prasad, 1995, Biopolymers.

Stereochemistry of peptides containing 1‐aminocycloheptane‐1‐carboxylic acid (Ac7c)

C. Toniolo, M. Crisma, P. Balaram, 2009 .

Hybrid polypeptides: gabapentin as a stereochemically constrained γ-amino acid residue.

P. Balaram, 2010, Biopolymers.

Comparison of helix-stabilizing effects of α,α-dialkyl glycines with linear and cycloalkyl side chains

I. Karle, P. Balaram, R. Rao, 2000 .

Helical conformations of hexapeptides containing N‐terminus diproline segments

P. Balaram, S. Aravinda, S. Raghothama, 2010, Biopolymers.

Conformational properties of hybrid peptides containing alpha- and omega-amino acids.

P. Balaram, R. Roy, P. Balaram, 2004, The journal of peptide research : official journal of the American Peptide Society.

A combined extended and helical backbone for Boc-(Ala-Leu-Ac7c-)2-OMe.

I. Karle, P. Balaram, S. Prasad, 2008, The journal of peptide research : official journal of the American Peptide Society.

C11/C9 helices in crystals of αβ hybrid peptides and switching structures between helix types by variation in the α-residue.

P. Balaram, K. Basuroy, Vasantham Karuppiah, 2014, Organic letters.

Structural studies of model peptides containing beta-, gamma- and delta-amino acids.

P. Balaram, A. Sengupta, K. Raja, 2006, Organic & biomolecular chemistry.

Alpha,beta hybrid peptides: a polypeptide helix with a central segment containing two consecutive beta-amino acid residues.

I. Karle, P. Balaram, R. Roy, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Expanding the peptide beta-turn in alphagamma hybrid sequences: 12 atom hydrogen bonded helical and hairpin turns.

C. Ramakrishnan, P. Balaram, Sunanda Chatterjee, 2009, Journal of the American Chemical Society.

Structural characterization of backbone-expanded helices in hybrid peptides: (αγ)n and (αβ)n sequences with unconstrained β and γ homologues of L-Val.

P. Balaram, B. Dinesh, N. Shamala, 2012, Angewandte Chemie.

β-Turn analogues in model αβ-hybrid peptides: structural characterization of peptides containing β(2,2)Ac6c and β(3,3)Ac6c residues.

P. Balaram, S. Raghothama, N. Shamala, 2012, Chemistry, an Asian journal.

Hybrid alphagamma polypeptides: structural characterization of a C12/C10 helix with alternating hydrogen-bond polarity.

P. Balaram, Sunanda Chatterjee, N. Shamala, 2008, Angewandte Chemie.

Solid state and solution conformations of a hybrid αγααγα hexapeptide. Characterization of a backbone expanded analog of the α‐polypeptide 310‐helix

P. Balaram, Sunanda Chatterjee, S. Raghothama, 2008, Biopolymers.

Expanding the polypeptide backbone: hydrogen-bonded conformations in hybrid polypeptides containing the higher homologues of α-amino acids

P. Balaram, Sunanda Chatterjee, R. Roy, 2007, Journal of The Royal Society Interface.

Hybrid Peptides: Expanding the β Turn in Peptide Hairpins by the Insertion of β‐, γ‐, and δ‐Residues

I. Karle, P. Balaram, R. Rai, 2007 .

Unconstrained homooligomeric γ-peptides show high propensity for C14 helix formation.

P. Balaram, S. Raghothama, B. Dinesh, 2013, Organic letters.

C12‐Helix Development in (αγ)n Sequences – Spectroscopic Characterization of Boc–[Aib–γ4(R)Val]–OMe Oligomers

P. Balaram, S. Raghothama, B. Dinesh, 2013 .

Hybrid peptide design. Hydrogen bonded conformations in peptides containing the stereochemically constrained gamma-amino acid residue, gabapentin.

P. Balaram, Sunanda Chatterjee, S. Aravinda, 2007, Journal of the American Chemical Society.

Conformational analysis of cyclolinopeptide A, a cyclic nonapeptide: Nuclear overhauser effect and energy minimization studies

C. Ramakrishnan, P. Balaram, D. Balasubramanian, 1989, Biopolymers.

C9 Helices and Ribbons in γ‐Peptides: Crystal Structures of Gabapentin Oligomers

P. Balaram, N. Shamala, P. Vasudev, 2005 .

Stereochemistry of Peptides and Polypeptides Containing Omega Amino Acids

P. Balaram, A. Banerjee, 1997 .

ω-Amino Acids in Peptide Design. Crystal Structures and Solution Conformations of Peptide Helices Containing a β-Alanyl-γ-Aminobutyryl Segment

I. Karle, P. Balaram, A. Banerjee, 1997 .

Peptide helices with pendant cycloalkane rings. Characterization of conformations of 1‐aminocyclooctane‐1‐carboxylic acid (Ac8c) residues in peptides

P. Balaram, S. Datta, R. Rathore, 2004, Journal of peptide science : an official publication of the European Peptide Society.

Aromatic-aromatic interactions in crystal structures of helical peptide scaffolds containing projecting phenylalanine residues.

Chittaranjan Das, I. Karle, P. Balaram, 2003, Journal of the American Chemical Society.

The stereochemistry of peptides containing alpha-aminoisobutyric acid.

P. Balaram, P Balaram, B V Prasad, 1984, CRC critical reviews in biochemistry.

Polypeptide helices in hybrid peptide sequences.

P. Balaram, A. Sengupta, K. Raja, 2005, Journal of the American Chemical Society.

Aggregation modes in sheets formed by protected β-amino acids and β-peptides

P. Balaram, V. Sabareesh, A. Sengupta, 2006 .

Beta-Hairpins Generated from Hybrid Peptide Sequences Containing both Alpha- and Beta-Amino Acids

I. Karle, P. Balaram, H. Gopi, 2002 .

Infinite pleated β-sheet formed by the β-hairpin Boc-β-Phe-β-Phe-d-Pro-Gly-β-Phe-β-Phe-OMe

I. Karle, P. Balaram, H. Gopi, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Alpha-helix and mixed 3(10)/alpha-helix in cocrystallized conformers of Boc-Aib-Val-Aib-Aib-Val-Val-Val-Aib-Val-Aib-OMe.

J. Flippen-Anderson, I. Karle, H. Balaram, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Comparison of the Effect of Five Guest Residues on the \beta-Sheet Conformation of Host ${(L-Val)}_n$ Oligopeptides

C. Toniolo, M. Crisma, H. Balaram, 1989 .

Hybrid Peptide Hairpins Containing α‐ and ω‐Amino Acids: Conformational Analysis of Decapeptides with Unsubstituted β‐, γ‐, and δ‐Residues at Positions 3 and 8

I. Karle, P. Balaram, H. Gopi, 2006 .

Peptide hybrids containing α- and β-amino acids: Structure of a decapeptide β-hairpin with two facing β-phenylalanine residues

I. Karle, P. Balaram, H. Gopi, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Gabapentin: a stereochemically constrained gamma amino acid residue in hybrid peptide design.

P. Balaram, Sunanda Chatterjee, N. Shamala, 2009, Accounts of chemical research.

Multiple conformational states in crystals and in solution in alphagamma hybrid peptides. Fragility of the C12 helix in short sequences.

P. Balaram, Sunanda Chatterjee, S. Raghothama, 2008, The Journal of organic chemistry.

Conformation of a 16-residue zervamicin IIA analog peptide containing three different structural features: 3(10)-helix, alpha-helix, and beta-bend ribbon.

J. Flippen-Anderson, I. Karle, P. Balaram, 1987, Proceedings of the National Academy of Sciences of the United States of America.

C12 helices in long hybrid (αγ)n peptides composed entirely of unconstrained residues with proteinogenic side chains.

P. Balaram, R. Sonti, S. Raghothama, 2014, Organic letters.

Promotion of folding in hybrid peptides through unconstrained γ residues: structural characterization of helices in (αγγ)n and (αγα)n sequences.

P. Balaram, B. Dinesh, N. Shamala, 2013, Angewandte Chemie.

Insertion of Methylene Units into the Turn Segment of Designed beta-Hairpin Peptides

P. Balaram, S. C. Shankaramma, S. Singh, 1999 .

Peptide Hairpins with Strand Segments Containing α- and β- Amino Acid Residues : Cross – Strand Aromatic Interactions of Facing Phe Residues.

Richard Gilardi, I. Karle, P. Balaram, 2005 .

Conformational choices for the stereochemically constrained γ‐amino acid residue gabapentin: Theoretical studies and correlation with experimental results

C. Ramakrishnan, P. Balaram, Sunanda Chatterjee, 2009, Biopolymers.

Control of Polypeptide Chain Folding and Assembly

P. Balaram, Rai Rajkishor, 2007 .

Stereochemistry of gabapentin and several derivatives: Solid state conformations and solution equilibria

P. Balaram, K. Raja, H. Sivaramakrishnan, 2003 .

Conformational interconversions in peptide beta-turns: analysis of turns in proteins and computational estimates of barriers.

J. Chandrasekhar, C. Ramakrishnan, P. Balaram, 1998, Journal of molecular biology.

Structural characterization of folded and extended conformations in peptides containing γ amino acids with proteinogenic side chains: crystal structures of γn, (αγ)n and γγδγ sequences

P. Balaram, S. Chandrappa, B. Dinesh, 2015 .

C−H⋅⋅⋅O Hydrogen Bond Mediated Chain Reversal in a Peptide Containing a γ‐Amino Acid Residue, Determined Directly from Powder X‐ray Diffraction Data

Roy L. Johnston, Kenneth D. M. Harris, Emilio Tedesco, 2002 .

Infrared studies on the conformation of synthetic alamethicin fragments and model peptides containing alpha-aminoisobutyric acid.

C. P. Rao, C. Rao, P. Balaram, 1980, Biochemistry.

Infrared spectroscopy as a probe for the development of secondary structure in the amino‐terminal segment of alamethicin

C. Rao, P. Balaram, R. Nagaraj, 1979, FEBS letters.

Crystallographic characterization of the α,γ C12 helix in hybrid peptide sequences

P. Balaram, S. Aravinda, K. Basuroy, 2016, Journal of peptide science : an official publication of the European Peptide Society.

Design of a peptide hairpin containing a central three-residue loop.

P. Balaram, R. Rai, S. Raghothama, 2006, Journal of the American Chemical Society.

Structural characterization of folded pentapeptides containing centrally positioned β(R)Val, γ(R)Val and γ(S)Val residues

P. Balaram, B. Dinesh, N. Shamala, 2012 .

Gabapentin: A Stereochemically Constrained γ Amino Acid Residue in Hybrid Peptide Design

P. Balaram, Sunanda Chatterjee, N. Shamala, 2010 .

Peptide δ-Turn: Literature Survey and Recent Progress.

C. Alemán, C. Toniolo, F. Formaggio, 2015, Chemistry.

The 310 helical conformation of a pentapeptide containing a-aminoisobutyric acid (Aib): X-ray crystal structure of Tos-(Aib)5 OMe

P. Balaram, R. Nagaraj, Padmanabhan Balaram, 1978 .

Conformational Properties of Hybrid Peptides Containing α‐ and ω‐Amino Acids

P. Balaram, R. Roy, 2004 .

Non-protein amino acids in peptide design

P. Balaram, R. Roy, S. Aravinda, 2003 .

Stereochemistry of Schellman motifs in peptides: Crystal structure of a hexapeptide with a C‐terminus 6 → 1 hydrogen bond

M. V. Uma, P. Balaram, S. Datta, 1999 .

De novo design: backbone conformational constraints in nucleating helices and beta-hairpins.

P. Balaram, 2008, The journal of peptide research : official journal of the American Peptide Society.

De novo design : backbone conformational constraints in nucleating helices and b-hairpins

P. Balaram, 1999 .

Molecular conformation and packing of peptide beta hairpins in the solid state: structures of two synthetic octapeptides containing 1-aminocycloalkane-1-carboxylic acid residues at the i+2 position of the beta turn.

P. Balaram, R. Rai, S. Aravinda, 2005, Chemistry.

Polymyxin B Nonapeptide: Conformations in Water and in the Lipopolysaccharide-Bound State Determined by Two-Dimensional NMR and Molecular Dynamics

P. Balaram, V. Mathan, S. Bhattacharjya, 1997 .

Solvent-induced beta-hairpin to helix conformational transition in a designed peptide.

S. Awasthi, P. Balaram, S. C. Shankaramma, 2001, Biopolymers.

Modular design of synthetic protein mimics. Crystal structure of two seven-residue helical peptide segments linked by .epsilon.-aminocaproic acid

Judith L. Flippen-Anderson, J. Flippen-Anderson, I. Karle, 1991 .

Apolar peptide models for conformational heterogeneity, hydration, and packing of polypeptide helices: Crystal structure of hepta‐ and octapeptides containing α‐aminoisobutyric acid

J. Flippen-Anderson, I. Karle, P. Balaram, 1990, Proteins.

Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.

P. Balaram, U. Raghavender, R. Rai, 2013, Organic & biomolecular chemistry.

Helix and hairpin nucleation in short peptides using centrally positioned conformationally constrained dipeptide segments.

P. Balaram, S. Chandrappa, R. Sonti, 2012, Organic & biomolecular chemistry.

Peptide hairpin nucleation with the obligatory Type I' beta-turn Aib-DPro segment.

P. Balaram, U. Raghavender, R. Rai, 2010, Organic & biomolecular chemistry.

Crystal structure of a hydrophobic 19-residue peptide helix containing three centrally located d amino acids

I. Karle, P. Balaram, H. Gopi, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Designed peptides with homochiral and heterochiral diproline templates as conformational constraints.

P. Balaram, Bhaswati Chatterjee, R. Rai, 2008, Chemistry.

Diproline templates as folding nuclei in designed peptides. Conformational analysis of synthetic peptide helices containing amino terminal Pro-Pro segments.

P. Balaram, R. Rai, S. Aravinda, 2006, Journal of the American Chemical Society.

Conformational interconversions in peptide β-turns: Discrimination between enantiomeric conformations by chiral perturbation

S. Banumathi, D. Velmurugan, P. Balaram, 1998 .

Peptide design. Helix–helix motifs in synthetic sequences

P. Balaram, A. Banerjee, S. Raghothama, 1997 .

Conformations and mitochondrial uncoupling activity of synthetic emerimicin fragments

P. Balaram, P. Raj, M. Das, 1988, Biopolymers.

Stereochemistry of α‐aminoisobutyric acid peptides in solution: Conformations of decapeptides with a central triplet of contiguous L‐amino acids

H. Balaram, P. Balaram, M. Sukumar, 1986 .

Probing the role of the C-H...O hydrogen bond stabilized polypeptide chain reversal at the C-terminus of designed peptide helices. Structural characterization of three decapeptides.

P. Balaram, S. Aravinda, N. Shamala, 2003, Journal of the American Chemical Society.

Peptide mimics for structural features in proteins. Crystal structures of three heptapeptide helices with a C-terminal 6-->1 hydrogen bond.

J. Flippen-Anderson, I. Karle, P. Balaram, 2009, International journal of peptide and protein research.

Termination of right handed helices in proteins by residues in left handed helical conformations

R Sowdhamini, H. A. Nagarajaram, R. Sowdhamini, 1993, FEBS letters.

Characterization of Helix Terminating Schellman Motifs in Peptides. Crystal Structure and Nuclear Overhauser Effect Analysis of a Synthetic Heptapeptide Helix

P. Balaram, A. Banerjee, S. Bhattacharjya, 1997 .

Heterogeneity and stability of helical conformations in peptides: crystallographic and NMR studies of a model heptapeptide

P. Balaram, A. Banerjee, S. Datta, 1996 .

Hydrogen-bond lengths in polypeptide helices: no evidence for short hydrogen bonds.

P. Balaram, S. Datta, S. Aravinda, 2004, Angewandte Chemie.

Facile transition between 310‐ and α‐helix: Structures of 8‐, 9‐, and 10‐residue peptides containing the ‐(Leu‐Aib‐Ala)2‐Phe‐Aib‐fragment

J. Flippen-Anderson, I. Karle, R. Gurunath, 1994, Protein science : a publication of the Protein Society.

Solvated helical backbones: X‐ray diffraction study of Boc‐Ala‐Leu‐Aib‐Ala‐Leu‐Aib‐OMe · H2O

J. Flippen-Anderson, I. Karle, P. Balaram, 1989, Biopolymers.

Monoclinic polymorph of Boc-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-OMe(anhydrous). Parallel packing of 3(10)-/alpha-helices and a transition of helix type.

J. Flippen-Anderson, I. Karle, P. Balaram, 2009, International journal of peptide and protein research.

Solution conformations of penta and heptapeptides containing repetitive α-aminoisobutyryl-l-alanyl and α -aminoisobutyryl-l-valyl sequences

P. Balaram, E. K. Vijayakumar, 1983 .

Molecular carpentry: piecing together helices and hairpins in designed peptides.

P. Balaram, C. Das, S. C. Shankaramma, 2001, Chemistry.

Homooligomeric β3(R)‐valine peptides: Transformation between C14 and C12 helical structures induced by a guest Aib residue

P. Balaram, S. Raghothama, B. Vasantha, 2017, Biopolymers.

Conformational choice at α,α‐Di‐n‐propylglycine residues: Helical or fully extended structures?

S. Banumathi, D. Velmurugan, P. Balaram, 2000 .

Entrapment of a water wire in a hydrophobic peptide channel with an aromatic lining.

P. Balaram, Bhaswati Chatterjee, U. Raghavender, 2011, Journal of Physical Chemistry B.

Hydrophobic peptide channels and encapsulated water wires.

P. Balaram, U. Raghavender, S. Aravinda, 2010, Journal of the American Chemical Society.

A Designed Three Stranded beta-Sheet Peptide as a Multiple beta-Hairpin Model

Chittaranjan Das, P. Balaram, C. Das, 1998 .

Tuning the β‐turn segment in designed peptide β‐hairpins: Construction of a stable type I′ β‐turn nucleus and hairpin–helix transition promoting segments

P. Balaram, R. Rai, S. Raghothama, 2007 .

Structure and assembly of designed beta-hairpin peptides in crystals as models for beta-sheet aggregation.

P. Balaram, C. Das, S. Aravinda, 2004, Biochemistry.

Designed beta-hairpin peptides with defined tight turn stereochemistry.

I. Karle, P. Balaram, C. Das, 2001, Biopolymers.

Omega amino acids in peptide design: incorporation into helices.

P. Balaram, A. Banerjee, S. Bhattacharjya, 1998, Biopolymers.

A designed beta-hairpin peptide in crystals.

I. Karle, S. Awasthi, P. Balaram, 1996, Proceedings of the National Academy of Sciences of the United States of America.

A designed beta-hairpin peptide.

S. Awasthi, P. Balaram, S. Raghothama, 1995, Biochemical and biophysical research communications.

A model for the interaction of trifluoroethanol with peptides and proteins.

P. Balaram, R. Rajan, P. Balaram, 2009, International journal of peptide and protein research.

Biradicals as ESR probes of conformations in model beta-turn peptides.

P. Balaram, P. Manoharan, M. Sukumar, 1995, Biochemical and biophysical research communications.

Pregabalin peptides: conformational comparison of γ3- and γ4-substituted γ-amino acids in αγααα pentapeptides

P. Balaram, S. Aravinda, N. Shamala, 2019, Amino Acids.

Hybrid ag Polypeptides : Structural Characterization of a C 12 / C 10 Helix with Alternating Hydrogen-Bond Polarity * *

P. Balaram, Sunanda Chatterjee, N. Shamala, 2008 .

Solid State and Solution Conformations of a Hybrid acaaca Hexapeptide . Characterization of a Backbone Expanded Analog of the a-Polypeptide 310-Helix

P. Balaram, Sunanda Chatterjee, S. Raghothama, 2008 .

Multiple Conformational States in Crystals and in Solution in rγ Hybrid Peptides. Fragility of the C12 Helix in Short Sequences

P. Balaram, Sunanda Chatterjee, S. Raghothama, 2008 .

Hybrid peptides: expanding the beta turn in peptide hairpins by the insertion of beta-, gamma-, and delta-residues.

I. Karle, P. Balaram, R. Rai, 2007, Chemistry.

Aqueous channels within apolar peptide aggregates: solvated helix of the alpha-aminoisobutyric acid (Aib)-containing peptide Boc-(Aib-Ala-Leu)3-Aib-OMe.2H2O.CH3OH in crystals.

J. Flippen-Anderson, I. Karle, P. Balaram, 1988, Proceedings of the National Academy of Sciences of the United States of America.

Conformational properties and aggregation of homo‐oligomeric β3(R)‐valine peptides in organic solvents

P. Balaram, S. Raghothama, B. Vasantha, 2017, Biopolymers.

Hydration and distortion of peptide helices in crystals. Alpha-helical structure of a dodecapeptide, Boc-(Ala-Leu-Aib)4-OMe.

J. Flippen-Anderson, I. Karle, P. Balaram, 2009, International journal of peptide and protein research.

Unfolding of an α‐helix in peptide crystals by solvation: Conformational fragility in a heptapeptide

J. Flippen-Anderson, I. Karle, P. Balaram, 1993, Biopolymers.

The crystal and molecular structure of the amino terminal tetrapeptide of alamethicin. A novel 310 helical conformation.

P. Balaram, R. Nagaraj, N. Shamala, 1977, Biochemical and biophysical research communications.

Sparsely populated residue conformations in protein structures: Revisiting “experimental” Ramachandran maps

C. Ramakrishnan, P. Balaram, Neha V. Kalmankar, 2014, Proteins.

Conformation of di‐n‐propylglycine residues (Dpg) in peptides: crystal structures of a type I′β‐turn forming tetrapeptide and an α‐helical tetradecapeptide

P. Balaram, R. Rai, S. Aravinda, 2008 .

Conformational and sequence signatures in beta helix proteins.

P. Iengar, P. Balaram, Padmanabhan Balaram, 2006, Structure.

Non-protein amino acids in the design of secondary structure scaffolds.

P. Balaram, R. Mahalakshmi, 2006, Methods in molecular biology.

Conformational and sequence signatures in beta helix proteins.

P. Iengar, P. Balaram, N. Joshi, 2006, Structure.

Disallowed Ramachandran conformations of amino acid residues in protein structures.

K. Gunasekaran, C. Ramakrishnan, P. Balaram, 1996, Journal of molecular biology.

NMR analysis of aromatic interactions in designed peptide beta-hairpins.

P. Balaram, R. Mahalakshmi, S. Raghothama, 2006, Journal of the American Chemical Society.

Conformations of synthetic alamethicin fragments. Evidence for 310 helical folding from 270-MHz hydrogen-1 nuclear magnetic resonance and circular dichroism studies.

P. Balaram, R. Nagaraj, 1981, Biochemistry.

Directing peptide conformation with centrally positioned pre-organized dipeptide segments: studies of a 12-residue helix and β-hairpin

P. Balaram, S. Chandrappa, R. Sonti, 2014, Amino Acids.

Aromatic interactions in model peptide β‐hairpins: Ring current effects on proton chemical shifts

P. Balaram, S. Aravinda, S. Raghothama, 2012, Biopolymers.

Conformations of heterochiral and homochiral proline‐pseudoproline segments in peptides: Context dependent cis–trans peptide bond isomerization

P. Balaram, U. Raghavender, S. Aravinda, 2009, Biopolymers.

Crystal structures of peptide enantiomers and racemates: Probing conformational diversity in heterochiral Pro‐Pro sequences

P. Balaram, Bhaswati Chatterjee, I. Saha, 2008, Biopolymers.

Tryptophan rich peptides: influence of indole rings on backbone conformation.

P. Balaram, A. Sengupta, R. Mahalakshmi, 2007, Biopolymers.

Peptide models of electrostatic interactions in proteins: NMR studies on two beta-turn tetrapeptides containing Asp-His and Asp-Lys salt bridges.

P. Balaram, D. Sahal, 1986, Biochemistry.

Comparison of helix-stabilizing effects of alpha,alpha-dialkyl glycines with linear and cycloalkyl side chains.

I. Karle, P. Balaram, R. Rao, 2000, Biopolymers.

Molecular conformation of alamethicin in dimethylsulfoxide solution A two-dimensional n.m.r. study

Anil Kumar, P. Balaram, K. Chandrasekhar, 2009 .

Alamethicin and related membrane channel forming polypeptides

P. Balaram, M. Mathew, P. Balaram, 2004, Molecular and Cellular Biochemistry.

The role of polar and facial amphipathic character in determining lipopolysaccharide-binding properties in synthetic cationic peptides

P. Balaram, S. David, S. Awasthi, 2000, Journal of endotoxin research.

Resolution of racemic gossypol and interaction of individual enantiomers with serum albumins and model peptides.

P. Balaram, D. S. Sampath, 1986, Biochimica et biophysica acta.

Cyclic peptide disulfides. Solution and solid-state conformation of Boc-Cys-Pro-Aib-Cys-NHMe with a disulfide bridge from Cys to Cys, a disulfide-bridged peptide helix

P. Balaram, A. Ravi, B. Prasad, 1983 .

Chain length effects on helix‐hairpin distribution in short peptides with Aib‐DAla and Aib‐Aib Segments

P. Balaram, S. Aravinda, S. Raghothama, 2011, Biopolymers.

Characterization of bent helical conformations in polymorphic forms of a designed 18-residue peptide containing a central Gly-Pro segment.

I. Karle, P. Balaram, S. Aravinda, 2012, Biopolymers.

Characterization of water wires inside hydrophobic tubular peptide structures.

P. Balaram, U. Raghavender, R. Rai, 2009, Journal of the American Chemical Society.

Fluoroalcohols as structure modifiers in peptides and proteins: hexafluoroacetone hydrate stabilizes a helical conformation of melittin at low pH.

P. Balaram, S. Bhattacharjya, J. Venkatraman, 1999, The journal of peptide research : official journal of the American Peptide Society.

"Teflon-coated peptides": hexafluoroacetone trihydrate as a structure stabilizer for peptides.

S. Awasthi, P. Balaram, S. Bhattacharjya, 1997, Biopolymers.

Stabilization of γ‐turn conformations in peptides by disulfide bridging

P. Balaram, R. Kishore, 1985 .

The crystal structure of benzyloxycarbonyl-(α-aminoisobutyryl)2-l-alanyl methyl ester

P. Balaram, R. Nagaraj, N. Shamala, 1980 .

Amino acid-lanthanide interactions. Crystal structures of lanthanide complexes of α- amino isobutyric acid (Aib), [La2(Aib)4(H2O)8](ClO4)6 and [Pr2(Aib)4(H2O)8]Cl6·H2O

P. Balaram, M. Nethaji, S. S. Krishnamurthy, 1994 .

AMINO ACID-LANTHANIDE INTERACTIONS. CRYSTAL STRUCTURES OF LANTHANIDE COMPLEXES OF a- AMINO ISOBUTYRIC ACID (Aib), (La,(Aib),(H,O),) (ClO& AND (Pr,(Aib),(H,O),)C1, Hz0

P. Balaram, M. Nethaji, S. S. Krishnamurthy, 1994 .

Infrared spectroscopic study of C7 intramolecular hydrogen bonds in peptides

C. Rao, P. Balaram, C. Rao, 1983, Biopolymers.

Determination of beta-turn conformation by laser Raman spectroscopy.

A. Tu, P. Balaram, R. Nagaraj, 1981, Biophysical journal.

Fluorescent probe and NMR studies of the aggregation of bile salts in aqueous solution

P. Balaram, M. Mathew, R. Narayanan, 1979 .

Conformations Of Peptides Containing 1-Aminocyclohexane-Carboxylic Acid (Acc6) - Crystal-Structures Of 2 Model Peptides

Claudio Toniolo, C. Toniolo, P. Balaram, 2009 .

Solid state and solution conformation of Boc-L-Met-Aib-L-Phe-OMe. Beta-turn conformation of a sequence related to an active chemotactic peptide analog.

C. Toniolo, P. Balaram, P. Raj, 2009, International journal of peptide and protein research.

Membrane channel-forming polypeptides. Aqueous phase aggregation and membrane-modifying activity of synthetic fluorescent alamethicin fragments.

P. Balaram, R. Nagaraj, M. Mathew, 1982, Journal of Biological Chemistry.

Membrane Channel-forming Polypeptides

P. Balaram, R. Nagaraj, M. Mathew, 1982 .

Combined electron transfer dissociation-collision-induced dissociation fragmentation in the mass spectrometric distinction of leucine, isoleucine, and hydroxyproline residues in Peptide natural products.

P. Balaram, Kallol Gupta, Mukesh Kumar, 2012, Journal of Proteome Research.

Solution conformation of a tetradecapeptide stabilized by two di‐n‐propyl glycine residues

P. Balaram, V. Sarojini, S. Ragothama, 2010, Journal of peptide science : an official publication of the European Peptide Society.

Interactions of the channel forming peptide alamethicin with artificial and natural membranes

P. Balaram, M. Das, 1984, Journal of Biosciences.

Characterization of a 22-residue peptide derived from a designed ion channel.

P. Balaram, M. Mathew, S. Seth, 1997, Biochimica et biophysica acta.

Membrane channel forming polypeptides. Molecular conformation and mitochondrial uncoupling activity of antiamoebin, an alpha-aminoisobutyric acid containing peptide.

P. Balaram, S. Raghothama, M. Das, 1986, Biochemistry.

Aggregation of apolar peptides in organic solvents. Concentration dependence of 1H‐nmr parameters for peptide NH groups in 310 helical decapeptide fragment of suzukacillin

P. Balaram, M. Iqbal, 1982 .

Unusual stability of a multiply nicked form of Plasmodium falciparum triosephosphate isomerase.

H. Balaram, S. Ray, P. Balaram, 1999, Chemistry & biology.

Cyclic peptide disulfides

P. Balaram, A. Ravi, 1983 .

Conformational analysis of small disulfide loops. Spectroscopic and theoretical studies on a synthetic cyclic tetrapeptide containing cystine.

P. Balaram, Y. Venkatachalapathi, B. Prasad, 1982, Biochemistry.

Molecular structure of a cyclic tetrapeptide disulfide. A novel 3(10) helical conformation with an S-S bridge.

P. Balaram, A. Ravi, B. Prasad, 1981, Biochemical and biophysical research communications.

THE USE OF D-AMINO ACIDS IN PEPTIDE DESIGN

P. Balaram, R. Mahalakshmi, 2006 .

Effects of organic solvents on protein structures: Observation of a structured helical core in hen egg‐white lysozyme in aqueous dimethylsulfoxide

P. Balaram, S. Bhattacharjya, P. Balaram, 1997, Proteins.

Hexafluoroacetone hydrate as a structure modifier in proteins: Characterization of a molten globule state of hen egg‐white lysozyme

P. Balaram, S. Bhattacharjya, 1997, Protein science : a publication of the Protein Society.

Cation binding to brain plasma membranes. An evaluation of the use of anionic fluorescent probes.

P. Balaram, K. Krishnan, 1976, Archives of biochemistry and biophysics.

PEPTIDE MODELS FOR THE BACTERIORHODOPSIN CHROMOPHORE. RETINYLIDENE‐LYSINE SYSTEMS CONTAINING ASPARTIC ACID AND SERINE RESIDUES

P. Balaram, E. K. Vijayakumar, 1984 .

Acyclic sugars: the ring-opening of 2-acetamido-2-deoxyhexopyranoses in trifluoroacetic acid

P. Balaram, V. Rao, M. Ranganathan, 1977 .

Conformational diversity in contryphans from Conus venom: cis-trans isomerisation and aromatic/proline interactions in the 23-membered ring of a 7-residue peptide disulfide loop.

Alex Rodriguez, P. Balaram, K. H. Gowd, 2013, Chemistry.

Synthesis and fluorescence properties of a probe for membrane anionic sites.

P. Balaram, R. Narayanan, 1976, Biochemical and biophysical research communications.

Regional differentiation in bull sperm plasma membranes.

P. Balaram, S. Vijayasarathy, 1982, Biochemical and biophysical research communications.

Interaction of cationic amphiphilic drugs with lipid A: implications for development of endotoxin antagonists.

P. Balaram, V. Mathan, S. David, 1994, Biochimica et biophysica acta.

Intramolecular backbone···backbone hydrogen bonds in polypeptide conformations. The other way around: ɛ‐turn

C. Alemán, C. Toniolo, F. Formaggio, 2017, Biopolymers.

Multiple conformational states of a Pro-Pro peptide. Solid-state and solution conformations of Boc-Aib-Pro-Pro-NHMe

H. Balaram, P. Balaram, B. Prasad, 1983 .

Circular dichroism studies of helical oligopeptides. Can 3(10) and alpha-helical conformations be chiroptically distinguished?

P. Balaram, E. K. Vijayakumar, T. Sudha, 2009, International journal of peptide and protein research.

Acyclic peptides as conformational models Crystal structure of Boc-Aib-Leu-Pro-NHMe± 2H2O

H. Balaram, B. Prasad, P. Balaram, 2009 .

Characterization of a hemoglobin variant: HbQ-India / IVS 1-1 [G>T]-β-thalassemia

P. Balaram, A. Mandal, Vijay S. Bhat, 2010, Indian Journal of Clinical Biochemistry.

Electrospray mass spectrometric characterization of hemoglobin Q (Hb Q-India) and a double mutant hemoglobin S/D in clinical samples.

P. Balaram, A. Mandal, Vijay S. Bhat, 2008, Clinical biochemistry.

Stereochemistry of peptides containing 1‐aminocyclopentanecarboxylic acid (Acc5): Solution and solid‐state conformations of Boc‐Acc5‐Acc5‐NHMe

C. Toniolo, P. Balaram, M. Sukumar, 1986 .

Stereochemistry of peptides containing 1‐aminocyclopentanecarboxylic acid (Acc5): Solution and solid‐state conformations of Boc‐Acc5‐Acc5‐NHMe

C. Toniolo, P. Balaram, M. Sukumar, 1986 .

Solution Phase Synthesis of Alamethicin I

P. Balaram, R. Nagaraj, 1981 .

Increased glutathionylated hemoglobin (HbSSG) in type 2 diabetes subjects with microangiopathy.

M. Rema, P. Balaram, M. Balasubramanyam, 2005, Clinical biochemistry.

Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site.

M. Murthy, P. Gayathri, H. Balaram, 2009, Acta crystallographica. Section D, Biological crystallography.

Structure of Plasmodium falciparum Triose-phosphate Isomerase-2-Phosphoglycerate Complex at 1.1-Å Resolution*

S. Parthasarathy, M. Murthy, K. Eaazhisai, 2003, Journal of Biological Chemistry.

Hydrophobic channels in crystals of an α-aminoisobutyric acid pentapeptide

P. Balaram, R. Nagaraj, N. Shamala, 1981 .

Formyl‐met—leu—phe induces chemotaxis and acrosomal enzyme release in bull sperm

P. Balaram, M. Iqbal, S. Vijayasarathy, 1980, FEBS letters.

Probing peptide libraries from Conus achatinus using mass spectrometry and cDNA sequencing: identification of delta and omega-conotoxins.

P. Iengar, P. Balaram, K. H. Gowd, 2008, Journal of mass spectrometry : JMS.

Conformationally constrained chemotactic peptide analogs of high biological activity

P. Balaram, H. Showell, R. Freer, 1984, FEBS letters.

A C-H· · ·O Hydrogen Bond Stabilized Polypeptide Chain Reversal Motif at the C Terminus of Helices in Proteins

M. Babu, P. Balaram, S. Singh, 2002 .

Inhibition of Plasmodium falciparum Triose-phosphate Isomerase by Chemical Modification of an Interface Cysteine

H. Balaram, P. Balaram, G. Ravindra, 2002, The Journal of Biological Chemistry.

Contryphan Genes and Mature Peptides in the Venom of Nine Cone Snail Species by Transcriptomic and Mass Spectrometric Analysis.

P. Balaram, J. B. Franklin, M. Vijayasarathy, 2017, Journal of proteome research.

Disulfide bond assignments by mass spectrometry of native natural peptides: cysteine pairing in disulfide bonded conotoxins.

P. Balaram, Kallol Gupta, Mukesh Kumar, 2010, Analytical chemistry.

De novo sequencing and disulfide mapping of a bromotryptophan-containing conotoxin by Fourier transform ion cyclotron resonance mass spectrometry.

Carol L Nilsson, Konkallu Hanumae Gowd, M. Emmett, 2006, Analytical chemistry.

Mammalian neuronal sodium channel blocker μ-conotoxin BuIIIB has a structured N-terminus that influences potency.

D. Yoshikami, R. Norton, P. Balaram, 2013, ACS chemical biology.

Distinct disulfide isomers of μ-conotoxins KIIIA and KIIIB block voltage-gated sodium channels.

D. Yoshikami, R. Norton, P. Balaram, 2012, Biochemistry.

Lipopeptides from the Banyan Endophyte, Bacillus subtilis K1: Mass Spectrometric Characterization of a Library of Fengycins

P. Balaram, H. Keharia, S. Thakur, 2012, Journal of The American Society for Mass Spectrometry.

Connecting Active‐Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme

M. Murthy, H. Balaram, P. Balaram, 2016, Chembiochem : a European journal of chemical biology.

A 1H-NMR study of bilirubin IX alpha solubilization by cholate micelles: application of nuclear Overhauser effects.

P. Balaram, K. Puranam, S. Raghothama, 1987, Biochimica et biophysica acta.

Identification of Conus Amadis Disulfide Isomerase: Minimum Sequence Length of Peptide Fragments Necessary for Protein Annotation{

P. Balaram, K. H. Gowd, K. S. Krishnan, 2007 .

Mammalian brain plasma membranes. Isolation, enzymatic, and chemical characterization.

P. Balaram, K. Krishnan, 1976, Experimental cell research.

Effect of amino acid substitutions at the subunit interface on the stability and aggregation properties of a dimeric protein: Role of Arg 178 and Arg 218 at the dimer interface of thymidylate synthase

D. Santi, P. Balaram, B. Gopal, 1999, Proteins.

Stabilisation of enzyme structures by inhibitors. A nuclear magnetic resonance study of the effect of phosphate on the acid unfolding of ribonuclease A.

P. Vithayathil, P. Balaram, M. Das, 2009, International journal of peptide and protein research.

Engineered dimer interface mutants of triosephosphate isomerase: the role of inter-subunit interactions in enzyme function and stability.

H. Balaram, P. Balaram, M. Banerjee, 2011, Protein engineering, design & selection : PEDS.

Synthetic peptides as inactivators of multimeric enzymes: inhibition of Plasmodium falciparum triosephosphate isomerase by interface peptides

H. Balaram, P. Balaram, K. Maithal, 2001, FEBS letters.

Cone Snail Glutaminyl Cyclase Sequences from Transcriptomic Analysis and Mass Spectrometric Characterization of Two Pyroglutamyl Conotoxins.

P. Balaram, M. Vijayasarathy, S. M. Basheer, 2018, Journal of proteome research.

Solution Structure of δ‐Am2766: A Highly Hydrophobic δ‐Conotoxin from Conus amadis That Inhibits Inactivation of Neuronal Voltage‐Gated Sodium Channels

S. Sikdar, P. Iengar, P. Balaram, 2005, Chemistry & biodiversity.

Disulfide engineering at the dimer interface of lactobacillus casei thymidylate synthase: Crystal structure of the T155C/E188C/C244T mutant

S. Parthasarathy, D. Santi, S. Ray, 2008, Protein science : a publication of the Protein Society.

Covalent tethering of the dimer interface annuls aggregation in thymidylate synthase

D. Santi, P. Balaram, S. Agarwalla, 1996, Protein science : a publication of the Protein Society.

Partial restoration of activity to Lactobacillus casei thymidylate synthase following inactivation by domain deletion.

B. Shoichet, D. Santi, P. Balaram, 1994, Biochemistry.

Registering α‐helices and β‐strands using backbone CH…O interactions

Sudheer Kumar Singh, P. Balaram, M. Madan Babu, 2003, Proteins.

Synthetic protein design: construction of a four-stranded beta-sheet structure and evaluation of its integrity in methanol-water systems.

P. Balaram, C. Das, P Balaram, 2000, The journal of peptide research : official journal of the American Peptide Society.

Beta-Hairpin nucleation by Pro-Gly beta-turns. Comparison of D-Pro-Gly and L-Pro-Gly sequences in an apolar octapeptide

S. Awasthi, P. Balaram, S. Raghothama, 1998 .

Conformational characteristics of asparaginyl residues in proteins.

R. Sowdhamini, C. Ramakrishnan, N. Srinivasan, 2009, International journal of peptide and protein research.

Orthogonal ββ motifs in proteins

R. Sowdhamini, C. Ramakrishnan, N. Srinivasan, 1992 .

Peptide design: Influence of a guest Aib‐Pro segment on the stereochemistry of an Oligo‐Val sequence—solution conformations and crystal structure of Boc‐(Val)2‐Aib‐Pro‐(Val)3‐OMe

J. Flippen-Anderson, I. Karle, H. Balaram, 1990, Biopolymers.

$^{13}C-n.m.r.$ studies of the conformational changes in proline oligomers brought about by lithium and calcium salts

P. Balaram, C. Rao, C. Rao, 1983 .

beta-Turn Analogues in Model a ss-Hybrid Peptides: Structural Characterization of Peptides Containing ss 2,2Ac6c and ss 3,3Ac6c Residues

P. Balaram, S. Raghothama, N. Shamala, 2012 .

A crystalline beta-hairpin peptide nucleated by a type I' Aib-D-Ala beta-turn: evidence for cross-strand aromatic interactions.

P. Balaram, H. Gopi, S. Aravinda, 2002, Angewandte Chemie.

Registering-Helices and-Strands Using Backbone C

M. Babu, P. Balaram, S. Singh, 2003 .

A C-H triplebond O hydrogen bond stabilized polypeptide chain reversal motif at the C terminus of helices in proteins.

M. Madan Babu, P. Balaram, S. Kumar Singh, 2002, Journal of molecular biology.

Folded conformations of antigenic peptides from riboflavin carrier protein in aqueous hexafluoroacetone

P. Adiga, P. Balaram, S. Bhattacharjya, 1998, Protein science : a publication of the Protein Society.

Nuclear Overhauser effects as probes of peptide structure. A diagnostic for left-handed helical conformations.

C. Ramakrishnan, P. Balaram, M. Sukumar, 1987, Biochemical and biophysical research communications.

Stabilization of β-turn conformations in Pro-X sequences by disulphide bridging. Synthesis and solution conformations of five cyclic cystine peptides

P. Balaram, A. Ravi, 1984 .

Consecutive beta-turn conformation of a synthetic model peptide corresponding to the active site of thioredoxin.

P. Balaram, A. Ravi, 1983, Biochimica et biophysica acta.

Ion channel formation by zervamicin-IIB

I. Karle, M. Sansom, P. Balaram, 2004, European Biophysics Journal.

Parallel and antiparallel aggregation of alpha-helices. Crystal structures of two apolar decapeptides X-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-OMe (X = Boc, Ac).

J. Flippen-Anderson, I. Karle, P. Balaram, 2009, International journal of peptide and protein research.

Helix aggregation in peptide crystals: Occurrence of either all parallel or antiparallel packing motifs for α‐helices in polymorphs of Boc‐Aib‐Ala‐Leu‐Ala‐Leu‐Aib‐Leu‐Ala‐Leu‐Aib‐OMe

J. Flippen-Anderson, I. Karle, P. Balaram, 1990, Biopolymers.

Mass spectrometric analysis of cyclotides from Clitoria ternatea: Xxx-Pro bond fragmentation as convenient diagnostic of Pro residue positioning.

P. Balaram, R. Venkatesan, Neha V. Kalmankar, 2021, Chemistry, an Asian journal.

Stage-specific profiling of Plasmodium falciparum proteases using an internally quenched multispecificity protease substrate.

H. Balaram, P. Balaram, P. Pattanaik, 2003, Biochemical and biophysical research communications.

Sequence of the SARS-CoV-2 spike transmembrane domain makes it inherently dynamic

S. Gosavi, P. Balaram, S. Lall, 2021, bioRxiv.

Metabolic enzymes as potential drug targets in Plasmodium falciparum.

H. Balaram, S. Ray, P. Balaram, 1997, The Indian journal of medical research.

Cone snail analogs of the pituitary hormones oxytocin/vasopressin and their carrier protein neurophysin. Proteomic and transcriptomic identification of conopressins and conophysins.

P. Balaram, Sanjeev Kumar, M. A. Venkatesha, 2020, Biochimica et biophysica acta. Proteins and proteomics.

Design of two-helix motifs in peptides: crystal structure of a system of linked helices of opposite chirality and a model helix-linker peptide.

I. Karle, P. Balaram, A. Banerjee, 1997, Folding & design.

Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site‐specific mutagenesis – distal effects on dimer stability

M. Murthy, H. Balaram, P. Balaram, 2011, The FEBS journal.

Mechanistic insights into an unusual side chain mediated N-Cα bond cleavage under collision induced dissociation conditions in the disulfide containing peptide conopressin.

P. Balaram, Sanjeev Kumar, S. Lall, 2020, Journal of the American Society for Mass Spectrometry.

Unusual fluorescence of W168 in Plasmodium falciparum triosephosphate isomerase, probed by single-tryptophan mutants.

H. Balaram, P. Balaram, P. Pattanaik, 2003, European journal of biochemistry.

A four stranded beta-sheet structure in a designed, synthetic polypeptide

P. Balaram, C. Das, S. Raghothama, 1999 .

Molecular conformation and biological interactions : G.N. Ramachandran festschrift

P. Balaram, S. Ramaseshan, 1991 .

Solid state and solution conformations of a helical peptide with a central gly‐gly segment

I. Karle, P. Balaram, A. Banerjee, 1996, Biopolymers.

Crystal structure of [Leu1]zervamicin, a membrane ion-channel peptide: implications for gating mechanisms.

J. Flippen-Anderson, I. Karle, P. Balaram, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Asparagine and glutamine differ in their propensities to form specific side chain‐backbone hydrogen bonded motifs in proteins

C. Ramakrishnan, P. Balaram, M. Banerjee, 2012, Proteins.

Structural basis for the hyperthermostability of an archaeal glutaminase induced by post-translational succinimide formation

H. Balaram, P. Balaram, S. Balasubramanian, 2021, bioRxiv.

Structural analysis of peptide helices containing centrally positioned lactic acid residues.

P. Balaram, C. Das, S. Aravinda, 2002, Biopolymers.

Hydrogen bonding in peptide helices. Analysis of two independent helices in the crystal structure of a peptide Boc-Val-Ala-Leu-Aib-Val-Ala-Phe-OMe.

P. Balaram, A. Banerjee, S. Datta, 2009, The journal of peptide research : official journal of the American Peptide Society.

Stereochemistry of linking segments in the design of helix–helix motifs in peptides. Crystallographic comparison of a glycyl–dipropylglycyl–glycyl segment in a tripeptide and a 14-residue peptide

P. Balaram, S. Datta, N. Shamala, 1997 .

Probing the role of highly conserved residues in triosephosphate isomerase – analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzyme

M. Murthy, H. Balaram, D. Bandyopadhyay, 2015, The FEBS journal.

Interactions of linear dicationic molecules with lipid A: structural requisites for optimal binding affinity

P. Balaram, V. Mathan, S. David, 1995 .

Perturbation of lipid structures by fluorescent probes

P. Balaram, K. Krishnan, 1975, FEBS letters.

Metal binding to pyridoxal derivatives. An NMR study of the interaction of Eu(III) with pyridoxal phosphate and pyridoxamine phosphate

C. Ramakrishnan, P. Balaram, B. Rao, 1979, Journal of Biosciences.

Sequencing of T-superfamily conotoxins from Conus virgo: Pyroglutamic acid identification and disulfide arrangement by MALDI mass spectrometry

P. Balaram, V. Sabareesh, A. Mandal, 2007, Journal of the American Society for Mass Spectrometry.

Tryptophan-containing peptide helices: interactions involving the indole side chain.

P. Balaram, P Balaram, A. Sengupta, 2005, The journal of peptide research : official journal of the American Peptide Society.

Bilirubin binding to polypeptides and chiral amines. Induced circular dichroism and fluorescence studies

P. Balaram, D. Marr-Leisy, Kasturi Lahiri, 2009 .

Spectroscopic studies on the interaction of bilirubin with symmetrical alkyl diamines

P. Balaram, K. Puranam, 1987, Journal of Biosciences.

An unusual C-H...O hydrogen bond mediated reversal of polypeptide chain direction in a synthetic peptide helix.

P. Balaram, C. Das, A. Pramanik, 2000, Biochemical and biophysical research communications.

Aromatic interactions in tryptophan-containing peptides: crystal structures of model tryptophan peptides and phenylalanine analogs.

P. Balaram, A. Sengupta, R. Mahalakshmi, 2008, The journal of peptide research : official journal of the American Peptide Society.

Modelling multiple disulphide loop containing polypeptides by random conformation generation. The test cases of alpha-conotoxin GI and endothelin I.

R. Sowdhamini, C. Ramakrishnan, P. Balaram, 1993, Protein engineering.

A right handed peptide helix containing a central double D-amino acid segment.

P. Balaram, Shrilakshmi Desiraju, S. Aravinda, 2002, Chemical communications.

The 310 Helical Conformation of the Amino Terminal Decapeptide of Suzukacillin. 270 MHz 'H NMR Evidence for Eight Intramolecular Hydrogen Bonds

P. Balaram, M. Iqbal, 1981 .

Context-dependent conformation of diethylglycine residues in peptides.

S. Banumathi, D. Velmurugan, P. Balaram, 2000, The journal of peptide research : official journal of the American Peptide Society.

Ambidextrous molecules: cylindrical peptide structures formed by fusing left- and right-handed helices.

I. Karle, P. Balaram, A. Banerjee, 1998, Biopolymers.

Conformational variability in short acyclic peptides. Stabilization of multiple beta-turn structures in organic solvents

S. Awasthi, P. Balaram, S. Raghothama, 1996 .

Peptides as bioorganic models

P. Balaram, 1984, Proceedings / Indian Academy of Sciences.

Stereochemistry of α‐aminoisobutyric acid peptides in solution: Helical conformations of protected decapeptides with repeating Aib‐L‐Ala and Aib‐L‐Val sequences

P. Balaram, E. K. S. Vijaya kumar, 1983, Biopolymers.

The crystal structure of a 310 helical decapeptide containing α‐aminoisobutyric acid

M. Vijayan, P. Balaram, M. Iqbal, 1983 .

Molecular structure of t‐butyloxycarbonyl‐Leu‐Aib‐Pro‐Val‐Aib‐methyl ester, a fragment of alamethicin and suzukacillin: A 310‐helical pentapeptide

P. Balaram, C. Rao, C. Rao, 1982 .

The helical conformations of 14- and 16-residue fragments of suzukacillin, a membrane channel-forming polypeptide.

P. Balaram, M. Iqbal, 1982, Biochimica et biophysica acta.

Helical conformations of three crystalline pentapeptide fragments of suzukacillin, a membrane channel forming polypeptide.

M. Vijayan, P. Balaram, R. Nagaraj, 1982, Biochemical and biophysical research communications.

Membrane channel forming polypeptides. 270-MHz proton magnetic resonance studies of the aggregation of the 11-21 fragment of suzukacillin in organic solvents.

P. Balaram, M. Iqbal, 1981, Biochemistry.

Membrane channel forming polypeptides. 270-MHz hydrogen-1 nuclear magnetic resonance studies on the conformation of the 11-21 fragment of suzukacillin.

P. Balaram, M. Iqbal, 1981, Biochemistry.

X‐Pro peptides: Synthesis and solution conformation of benzyloxycarbonyl‐(Aib‐Pro)4methyl ester. Evidence for a novel helical structure

P. Balaram, Y. Venkatachalapathi, Y. V. Venkatachalapathi, 1981 .

Temperature dependence of peptide NH chemical shifts in benzene: Delineation of solvent‐shielded and exposed amide protons

P. Balaram, Y. Venkatachalapathi, 1981 .

Structure of cyclo(‐α‐aminoisobutyryl‐l‐phenylalanyl‐), C13H16N2O2

S. Ramakumar, K. Suguna, P. Balaram, 1985 .

Cystine peptides: disulfide conformations in 14-membered loops investigated by Raman spectroscopy and circular dichroism

A. Tu, P. Balaram, R. Kishore, 2009 .

Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state.

S. Parthasarathy, M. Murthy, H. Balaram, 2002, Acta crystallographica. Section D, Biological crystallography.

Conformational transitions in a Pro-Pro peptide on dissolution of single crystals.

H. Balaram, P. Balaram, B. V. Enkatara Prasad, 1982, Biochemical and biophysical research communications.

Aggregation studies in crystals of apolar helical peptides: Boc-Aib-Val-Ala-Leu-Aib-Val-Ala-Leu-Aib-OMe.

J. Flippen-Anderson, I. Karle, P. Balaram, 2009, International journal of peptide and protein research.

Peptide design: crystal structure of a helical peptide module attached to a potentially nonhelical amino terminal segment.

I. Karle, P. Balaram, R. Rao, 1998, Biopolymers.

Effects of End Group and Aggregation on Helix Conformation: Crystal Structure of Ac‐(Aib‐Val‐Ala‐Leu)2‐Aib‐ OMe

I. Karle, P. Balaram, K. Uma, 1996, Journal of peptide science : an official publication of the European Peptide Society.

Conformation of the flexible bent helix of Leu1‐zervamicin in crystal C and a possible gating action for ion passage

J. Flippen-Anderson, I. Karle, P. Balaram, 1994, Biopolymers.

Helix packing of leucine‐rich peptides: A parallel leucine ladder in the structure of Boc‐Aib‐Leu‐Aib‐Aib‐Leu‐Leu‐Leu‐Aib‐Leu‐Aib‐OMe

J. Flippen-Anderson, I. Karle, P. Balaram, 1992, Proteins.

Modular design of synthetic protein mimics. Characterization of the helical conformation of a 13-residue peptide in crystals.

J. Flippen-Anderson, I. Karle, P. Balaram, 1989, Biochemistry.

Type II β‐turn conformation of pivaloyl‐L‐prolyl‐α‐aminoisobutyryl‐N‐methylamide: Theoretical, spectroscopic, and X‐ray studies

H. Balaram, P. Balaram, B. Prasad, 1982 .

Structural and thermodynamic consequences of introducing alpha-aminoisobutyric acid in the S peptide of ribonuclease S.

S. Awasthi, R. Varadarajan, G. Ratnaparkhi, 2000, Protein engineering.

A C-H center dot center dot center dot O hydrogen bond stabilized polypeptide chain reversal motif at the C terminus of helices in proteins

M. Babu, P. Balaram, K. Singh, 2002 .

Fluorescent probe studies of mixed micelles of phospholipids and bile salts. Effect of cholesterol incorporation.

P. Balaram, R. Narayanan, R. Paul, 1980, Biochimica et biophysica acta.

Design and construction of an open multistranded beta-sheet polypeptide stabilized by a disulfide bridge.

P. Balaram, G. A. Nagana Gowda, Padmanabhan Balaram, 2002, Journal of the American Chemical Society.

Stereochemical constraints in peptide design: Analysis of the influence of a disulfide bridge and an α‐aminoisobutyryl residue on the conformation of a hexapeptide

P. Balaram, R. Kishore, K. Uma, 1993, Biopolymers.

Towards the design of structural mimics for proteins using helical peptide modules

I. Karle, P. Balaram, K. Lima, 1991 .

Cystine peptides. Antiparallel beta-sheet conformation of the cyclic biscystine peptide [Boc-Cys-Ala-Cys-NHCH3]2.

J. Flippen-Anderson, I. Karle, P. Balaram, 2009, International journal of peptide and protein research.

Simultaneous observation of positive and negative nuclear Overhauser effects in oligopeptides due to segmental motion.

H. Balaram, P. Balaram, S. Raghothama, 1988, Biochemical and biophysical research communications.

Cystine Peptides. The Antiparallel \beta -Sheet Conformation of Two Synthetic Cyclic Bis( cystine peptides)

P. Balaram, Anilesh Kumar, R. Kishore, 1985 .

X-Pro peptides. A theoretical study of the hydrogen bonded conformations of (α-aminoisobutyryl-l-prolyl)n sequences

P. Balaram, BV Venkataram Prasad, B. Prasad, 1982 .

Crystal and molecular structure of benzyloxycarbonyl‐α‐aminoisobutyryl‐L‐prolyl methylamide: The observation of an X2‐Pro3 Type III β‐Turn

R. Chandrasekaran, P. Balaram, R. Nagaraj, 1979 .

Stereochemically Constrained Linear Peptides. Conformations of Peptides Containing \alpha-Aminoisobutyric Acid

P. Balaram, R. Nagaraj, N. Shamala, 1979 .

A fluorescent probe study of the solubilisation of cholesterol by bile salt-phospholipid micelles.

P. Balaram, R. Paul, 1978, Biochemical and biophysical research communications.

Identification, Purification and Mass Spectrometric Characterization of Two Novel Cyclic Peptides from Clitoria ternatea

P. Balaram, S. Sudarslal, K. P. Laladhas, 2015 .

Parallel zippers formed by alpha-helical peptide columns in crystals of Boc-Aib-Glu(OBzl)-Leu-Aib-Ala-Leu-Aib-Ala-Lys(Z)-Aib-OMe.

J. Flippen-Anderson, I. Karle, P. Balaram, 1990, Proceedings of the National Academy of Sciences of the United States of America.

The design and construction of synthetic protein mimics

P. Balaram, 1992 .

Conformational flexibility in enkephalins: Solvent dependent transitions in peptides with Gly‐Gly segments detected by circular dichroism

P. Balaram, T. Sudha, 1981, FEBS letters.

Directing peptide conformation with centrally positioned pre-organized dipeptide segments: studies of a 12-residue helix and β-hairpin

P. Balaram, S. Chandrappa, R. Sonti, 2015, Amino Acids.

Conformational analysis of a 20-membered cyclic peptide disulfide from Conus virgo with a WPW segment: evidence for an aromatic-proline sandwich.

P. Balaram, K. H. Gowd, R. Sonti, 2014, Chemistry.

Ab initio structure determination of a peptideβ-turn from powder X-ray diffraction data

Roy L. Johnston, Kenneth D. M. Harris, Giles W. Turner, 2001 .

Crystal structures of a nonapeptide helix containing alpha, alpha-di-n-butylglycine (Dbg), Boc-Gly-Dbg-Ala-Val-Ala-Leu-Aib-Val-Leu-OMe.

I. Karle, R. Gurunath, P. Balaram, 2009, International journal of peptide and protein research.

Conformation-activity correlations for chemotactic tripeptide analogs incorporating dialkyl residues with linear and cyclic alkyl sidechains at position 2.

P. Balaram, E L Becker, P Balaram, 2009, International journal of peptide and protein research.

β‐Turn conformations in crystal structures of model peptides containing α,α‐Di‐n‐propylglycine and α,α‐Di‐n‐butylglycine

C. Toniolo, M. Crisma, P. Balaram, 1995, Biopolymers.

Revisiting the Mechanism of the Triosephosphate Isomerase Reaction: The Role of the Fully Conserved Glutamic Acid 97 Residue

H. Balaram, P. Balaram, M. Murthy, 2011, Chembiochem : a European journal of chemical biology.

A nuclear magnetic resonance study of the interaction of serotonin with gangliosides

P. Balaram, K. Krishnan, P. Balaram, 1976, FEBS letters.

Synthetic peptide models for protein secondary structures. Beta-sheet formation in acyclic cystine peptides.

H. Balaram, P. Balaram, K. Uma, 2009, International journal of peptide and protein research.

Internal water bridge and antiparallel sheet in the structure of benzyloxycarbonyl‐l‐alanyl‐d‐phenylalanyl‐l‐proline monohydrate

M. Vijayan, P. Balaram, R. Nagaraj, 1981 .

Facile Diketopiperazine Formation from Dipeptides Containing a-Aminoisobutyric Acid. Conformational Factors Influencing Cyclisation

P. Balaram, R. Nagaraj, 1977 .

Analysis of short interproton distances in proline peptides as a guide in the interpretation of Nuclear Overhauser Effects

R. Sowdhamini, C. Ramakrishnan, P. Balaram, 1988 .

Analysis of short loops connecting secondary structural elements in proteins

R. Sowdhamini, C. Ramakrishnan, N. Srinivasan, 1991 .

The crystal structure of the amino-terminal pentapeptide of suzukacillin. Occurrence of a four-fold peptide helix

M. Vijayan, P. Balaram, M. Iqbal, 1983 .

Cone snail prolyl-4-hydroxylase α-subunit sequences derived from transcriptomic data and mass spectrometric analysis of variable proline hydroxylation in C. amadis venom.

P. Balaram, M. Vijayasarathy, 2019, Journal of proteomics.

De novo protein design: crystallographic characterization of a synthetic peptide containing independent helical and hairpin domains.

I. Karle, P. Balaram, C. Das, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Crystal structure of the channel-forming polypeptide antiamoebin in a membrane-mimetic environment.

I. Karle, P. Balaram, M. A. Perozzo, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Parallel packing of alpha-helices in crystals of the zervamicin IIA analog Boc-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-OMe.2H2O.

I. Karle, P. Balaram, M. Sukumar, 1986, Proceedings of the National Academy of Sciences of the United States of America.

A helical peptide containing a majority of valyl residues. Crystal structure of t-butyloxycarbonyl-(L-valyl-α-aminoisobutyryl) 3 -L-valyl methyl ester monohydrate

M. Vijayan, P. Balaram, E. K. Vijayakumar, 2009 .

Structures of Pivaloyl-L-prolyl-N-methyl-D- phenylalaninamide and Pivaloyl-L-prolyl-N-methyl-D-valinamide

C. Toniolo, H. Balaram, P. Balaram, 1988 .

Structural Chemistry of Peptides Containing Backbone Expanded Amino Acid Residues: Conformational Features of β,γ, and Hybrid Peptides

P. Balaram, Sunanda Chatterjee, N. Shamala, 2011 .

Analysis of the binding of polymyxin B to endotoxic lipid A and core glycolipid using a fluorescent displacement probe.

P. Balaram, V. Mathan, S. David, 1992, Biochimica et biophysica acta.

Detection of the protein dimers, multiple monomeric states and hydrated forms of Plasmodium falciparum triosephosphate isomerase in the gas phase.

M. Murthy, P. Gayathri, P. Balaram, 2009, Protein engineering, design & selection : PEDS.

Structural analysis of synthetic peptide fragments from EmrE, a multidrug resistance protein, in a membrane-mimetic environment.

P. Balaram, G. A. Nagana Gowda, J. Venkatraman, 2002, Biochemistry.

Unexpected functional implication of a stable succinimide in the structural stability of Methanocaldococcus jannaschii glutaminase

H. Balaram, P. Balaram, Kallol Gupta, 2016, Nature Communications.

A reinvestigation of chlortetracycline fluorescence: effect of pH, metal ions, and environment

P. Balaram, M. Mathew, 1980 .

ROTATIONAL ISOMERISM ABOUT THE Cα-CO BOND IN PROLINE DERIVATIVES

P. Balaram, R. Nagaraj, Y. Venkatachalapathi, 2009 .

Science and Engineering, Theory and Experiment

P. Balaram, 2009 .

Synthetic interface peptides as inactivators of multimeric enzymes: inhibitory and conformational properties of three fragments from Lactobacillus casei thymidylate synthase.

P. Balaram, S. Bhattacharjya, P Balaram, 1998, Biochemistry.

Crystal state conformation of three model monomer units for the β‐bend ribbon structure

C. Toniolo, M. Crisma, P. Balaram, 1991 .

Effects of membrane channel-forming polypeptides on mitochondrial oxidative phosphorylation. A comparison of alamethicin, gramicidin A, melittin and tetraacetyl melittin.

P. Balaram, A. Basu, M. Das, 1985, Biochemistry international.

Stereochemical analysis of the antigenic tip of the V3 loop peptide of HIV-1 gp120.

C. Ramakrishnan, P. Balaram, K. Gunasekaran, 2009, International journal of peptide and protein research.

De novo design of a five-stranded β-sheet anchoring a metal-ion binding site

P. Balaram, J. Venkatraman, R. Sudha, 2001 .

Mass spectrometric identification of bromotryptophan containing conotoxin sequences from the venom of C. amadis

P. Balaram, M. Vijayasarathy, 2018, Toxicon : official journal of the International Society on Toxinology.

Faculty Opinions recommendation of Design of a novel globular protein fold with atomic-level accuracy.

P. Balaram, 2003 .

Stabilization of β-turn conformations in enkephalins

P. Balaram, T. Sudha, 1983 .

A rapid procedure for the resolution of racemic gossypol

P. Balaram, D. S. Sampath, 1986 .

Peptide hairpins with strand segments containing alpha- and beta-amino acid residues: cross-strand aromatic interactions of facing Phe residues.

I. Karle, P. Balaram, H. Gopi, 2005, Biopolymers.

Modular design of synthetic protein mimics. Crystal structures, assembly, and hydration of two 15- and 16-residue apolar, leucyl-rich helical peptides

J. Flippen-Anderson, I. Karle, P. Balaram, 1990 .

Racemization at proline residues during peptide bond formation : A study of diastereomeric mixtures of synthetic alamethicin fragments by 270 MHz 1H NMR

P. Balaram, R. Nagaraj, 1981 .

Effects of End Group and Aggregation on Helix Conformation: Crystal Structure of Ac‐(Aib‐Val‐Ala‐Leu)2‐Aib‐ OMe

J. Flippen-Anderson, I. Karle, P. Balaram, 1996, Journal of peptide science : an official publication of the European Peptide Society.

Observation of a mixed antiparallel and parallel beta-sheet motif in the crystal structure of Boc-Ala-Ile-Aib-OMe.

R. Gurunath, P. Balaram, S. Datta, 2009, International journal of peptide & protein research.

Conformational analysis of cyclolinopeptide A, a cyclic nonapeptide: Nuclear overhauser effect and energy minimization studies

C. Ramakrishnan, P. Balaram, D. Balasubramanian, 1989, Biopolymers.

Structures of unliganded and inhibitor complexes of W168F, a Loop6 hinge mutant of Plasmodium falciparum triosephosphate isomerase: observation of an intermediate position of loop6.

M. Murthy, K. Eaazhisai, H. Balaram, 2004, Journal of molecular biology.

Increased glutathionylated hemoglobin (HbSSG) in type 2 diabetes subjects with microangiopathy.

M. Rema, P. Balaram, M. Balasubramanyam, 2005, Clinical biochemistry.

Mass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii.

H. Balaram, P. Balaram, Kallol Gupta, 2011, Rapid communications in mass spectrometry : RCM.

Peptide models for b-turns.A circular dichroism study

G. Fasman, M. Crisma, H. Balaram, 2009 .

Structural chemistry and membrane modifying activity of the fungal polypeptides zervamicins, antiamoebins and efrapeptins

P. Balaram, M. Sukumar, K. Krishna, 1990 .

Homooligomeric β3(R)‐valine peptides: Transformation between C14 and C12 helical structures induced by a guest Aib residue

P. Balaram, S. Raghothama, B. Vasantha, 2017, Biopolymers.

Unconstrained homooligomeric γ-peptides show high propensity for C14 helix formation.

P. Balaram, S. Raghothama, B. Dinesh, 2013, Organic letters.

Crystal structures of diketopiperazines containing α‐aminoisobutyric acid: Cyclo(Aib‐Aib) and cyclo(Aib‐L‐Ile)

S. Ramakumar, K. Suguna, P. Balaram, 1982 .

Crystal Structures of a New Polymorphic Form of Gabapentin Monohydrate and the E and Z Isomers of 4‐Tertiarybutylgabapentin

P. Balaram, S. Aravinda, K. Nagarajan, 2009, Chemical biology & drug design.

Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals.

P. Balaram, U. Raghavender, R. Rai, 2013, Organic & biomolecular chemistry.

Synthetic peptide helices in crystals: Structure and antiparallel and skewed packing motifs for α‐helices in two isomeric decapeptides

J. Flippen-Anderson, I. Karle, P. Balaram, 1990, Biopolymers.

NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded β-sheet peptide.

P. Balaram, R. Sonti, S. Ragothama, 2012, Journal of Physical Chemistry B.

De novo protein design: crystallographic characterization of a synthetic peptide containing independent helical and hairpin domains.

P. Balaram, I. L. Karle, Chittaranjan Das, 2000, Proceedings of the National Academy of Sciences of the United States of America.

NMR Analysis of a Conformational Transition in an Acyclic Peptide. Model System for Studying Helix Unfolding

P. Balaram, S. Raghothama, M. Chaddha, 1996 .

Structural studies of the hen's egg lipovitellins. NMR and fluorescence investigations

P. Balaram, S. Mahadevan, D. N. Rao, 1978 .

Nonstandard Amino Acids in Conformational Design of Peptides. Helical Structures in Crystals of 5-10 Residue Peptides Containing Dipropylglycine and Dibutylglycine

I. Karle, P. Balaram, S. Prasad, 1994 .

Coexistence of Folded and Extended Conformations of a Tripeptide Containing α,α-Di-n-propylglycine in Crystals

D. Velmurugan, P. Balaram, E. Subramanian, 1994 .

Identification of Conus amadis disulfide isomerase: minimum sequence length of peptide fragments necessary for protein annotation.

P. Balaram, K. H. Gowd, K. S. Krishnan, 2007, Molecular bioSystems.

Fluorescent hydrophobic peptide fragments of emerimicin. Models for the study of peptide aggregation and interactions with lipids and proteins.

P. Balaram, R. Nagaraj, 1979, Biochemical and biophysical research communications.

Accommodation of a D‐Phe residue into a right‐handed 310‐helix: Structure of Boc‐D‐Phe‐(Aib)4‐Gly‐L‐Leu‐(Aib)2‐Ome, an analogue of the amino terminal segment of antiamoebins and emerimicins

J. Flippen-Anderson, I. Karle, P. Balaram, 1993, Biopolymers.

A novel 13 residue acyclic peptide from the marine snail, Conus monile, targets potassium channels.

S. Sikdar, P. Balaram, S. Sarma, 2004, Biochemical and biophysical research communications.

Promotion of folding in hybrid peptides through unconstrained γ residues: structural characterization of helices in (αγγ)n and (αγα)n sequences.

P. Balaram, B. Dinesh, N. Shamala, 2013, Angewandte Chemie.

Structural characterization of backbone-expanded helices in hybrid peptides: (αγ)n and (αβ)n sequences with unconstrained β and γ homologues of L-Val.

P. Balaram, B. Dinesh, N. Shamala, 2012, Angewandte Chemie.

Peptide design. Structural evaluation of potential nonhelical segments attached to helical modules.

I. Karle, R. Gurunath, P. Balaram, 1995 .