G. Otting

发表

Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling.

K. Wüthrich, T. Szyperski, H. Senn, 1989, Biochemistry.

Sequence-specific and stereospecific assignment of methyl groups using paramagnetic lanthanides.

N. Dixon, G. Otting, T. Huber, 2007, Journal of the American Chemical Society.

Protein hydration in aqueous solution.

K Wüthrich, G Otting, K. Wüthrich, 1992, Faraday discussions.

Discovery of a Non-Peptidic Inhibitor of West Nile Virus NS3 Protease by High-Throughput Docking

David Beer, Amedeo Caflisch, Danzhi Huang, 2009, PLoS neglected tropical diseases.

Homeodomain-DNA recognition

Kurt Wüthrich, Markus Affolter, Alexander F. Schier, 1994, Cell.

Solution structure of the DNA-binding domain and model for the complex of multifunctiona hexameric arginine represser with DNA

M. Nilges, G. Otting, J. Carey, 1997, Nature Structural Biology.

Organic solvents identify specific ligand binding sites on protein surfaces

G. Otting, E. Liepinsh, 1997, Nature Biotechnology.

Water Molecules in DNA Recognition II: A Molecular Dynamics View of the Structure and Hydration of the trp Operator

W F van Gunsteren, G Otting, W. V. van Gunsteren, 1998 .

Saposin fold revealed by the NMR structure of NK-lysin

Gottfried Otting, Edvards Liepinsh, J. Ruysschaert, 1997, Nature Structural Biology.

Lipid membrane binding of NK‐lysin

E. Goormaghtigh, J. Ruysschaert, G. Otting, 1998, FEBS letters.

Solution structure and dynamics of PEC-60, a protein of the Kazal type inhibitor family, determined by nuclear magnetic resonance spectroscopy.

G Otting, V. Mutt, K. Berndt, 1994, Journal of molecular biology.

Solution conformations of a linked construct of the Zika virus NS2B‐NS3 protease

G. Otting, C. Klein, B. Graham, 2017, Antiviral research.

Binding mode of the activity‐modulating C‐terminal segment of NS2B to NS3 in the dengue virus NS2B–NS3 protease

G. Otting, Wan-Na Chen, B. Graham, 2014, The FEBS journal.

Small neutral Gd(iii) tags for distance measurements in proteins by double electron-electron resonance experiments.

G. Otting, D. Goldfarb, J. Swarbrick, 2018, Physical chemistry chemical physics : PCCP.

Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets.

Christoph Nitsche, Thomas Huber, Gottfried Otting, 2016, Journal of the American Chemical Society.

The dengue virus NS2B–NS3 protease retains the closed conformation in the complex with BPTI

G. Otting, Wan-Na Chen, B. Graham, 2014, FEBS letters.

Synthesis of (±)-Panduratin A and Related Natural Products Using the High Pressure Diels–Alder Reaction

G. Otting, M. Coote, Junming Ho, 2013 .

Cell-free transcription/translation from PCR-amplified DNA for high-throughput NMR studies.

N. Dixon, G. Otting, S. Vasudevan, 2007, Angewandte Chemie.

NMR Analysis of the Dynamic Exchange of the NS2B Cofactor between Open and Closed Conformations of the West Nile Virus NS2B-NS3 Protease

G. Otting, S. Vasudevan, X. Su, 2009, PLoS neglected tropical diseases.

Origin of τ2 and τ2 ridges in 2D NMR spectra and procedures for suppression

Kurt Wüthrich, Gerhard Wagner, Gottfried Otting, 1986 .

Protein hydration in aqueous solution.

K Wüthrich, G Otting, K. Wüthrich, 1991, Science.

NMR Detection of Hydration Water in the Intermolecular Interface of a Protein-DNA Complex.

G. Otting, Y. Qian, K. Wuethrich, 1993 .

Mosquito-Derived Anophelin Sulfoproteins Are Potent Antithrombotics

G. Otting, R. Payne, B. Parker, 2018, ACS central science.

Tracking Conformational Changes in Calmodulin in Vitro, in Cell Extract, and in Cells by Electron Paramagnetic Resonance Distance Measurements.

S. Albeck, T. Unger, G. Otting, 2019, Chemphyschem : a European journal of chemical physics and physical chemistry.

Alignment of Biological Macromolecules in Novel Nonionic Liquid Crystalline Media for NMR Experiments

Gottfried Otting, G. Otting, Markus Rückert and, 2000 .

Paramagpy: software for fitting magnetic susceptibility tensors using paramagnetic effects measured in NMR spectra

G. Otting, T. Huber, H. Orton, 2019, Magnetic Resonance.

Pseudocontact shifts in biomolecular NMR using paramagnetic metal tags.

G. Otting, Christoph Nitsche, 2017, Progress in nuclear magnetic resonance spectroscopy.

4,4'-dithiobisdipicolinic acid: a small and convenient lanthanide binding tag for protein NMR spectroscopy.

G. Otting, T. Huber, Xinying Jia, 2011, Chemistry.

Integron-associated Mobile Gene Cassettes Code for Folded Proteins : The Structure of Bal 32 a , a NewMember of the Adaptable a C b Barrel Family

N. Dixon, Z. Dosztányi, P. Curmi, 2005 .

Integron-associated mobile gene cassettes code for folded proteins: The structure of Bal32a, a new member of the adaptable α + β barrel family

N. Dixon, Z. Dosztányi, P. Curmi, 2005 .

Protein engineering with unnatural amino acids.

G. Otting, C. Jackson, William H. Zhang, 2013, Current opinion in structural biology.

Critical Review Cell-free Synthesis of 15 N-Labeled Proteins for NMR Studies

N. Dixon, G. Otting, K. Ozawa, 2005 .

Protein structure and interactions by combined use of sequential NMR assignments and isotope labeling

H. Senn, G. Otting, K. Wuethrich, 1987 .

Radiation damping on cryoprobes.

G. Otting, Dmitry Shishmarev, D. Shishmarev, 2011, Journal of magnetic resonance.

Effect of protein stabilization on charge state distribution in positive- and negative-ion electrospray ionization mass spectra

N. Dixon, G. Otting, M. Sheil, 2007, Journal of the American Society for Mass Spectrometry.

Numbat: an interactive software tool for fitting Δχ-tensors to molecular coordinates using pseudocontact shifts

G. Otting, T. Huber, C. Schmitz, 2008, Journal of biomolecular NMR.

Cell-free expression of natively folded hydrophobins.

G. Otting, M. Sunde, A. Kwan, 2020, Protein expression and purification.

Strategies for measurements of pseudocontact shifts in protein NMR spectroscopy.

G. Otting, Michael John, 2007, Chemphyschem : a European journal of chemical physics and physical chemistry.

A DQ/ZQ NMR Experiment for the Determination of the Signs of SmallJ(1H,13C) Coupling Constants in Linear Spin Systems

G. Otting, 1997 .

3D Computational Modeling of Proteins Using Sparse Paramagnetic NMR Data.

G. Otting, T. Huber, K. B. Pilla, 2017, Methods in molecular biology.

Generation of pseudocontact shifts in proteins with lanthanides using small "clickable" nitrilotriacetic acid and iminodiacetic acid tags.

G. Otting, B. Graham, K. Tuck, 2015, Chemistry.

Site-specific Labelling with a Metal Chelator for Protein-structure Refinement

G. Otting, A. Leonchiks, G. Pintacuda, 2004, Journal of biomolecular NMR.

InOOH-mediated Intergrown Heterojunctions for Enhanced Photocatalytic Performance: Assembly and Interfacial Charge Carrier Transferring

T. Frankcombe, G. Otting, Borui Liu, 2022, Chemical Engineering Journal.

Cell-free protein synthesis for analysis by NMR spectroscopy.

N. Dixon, G. Otting, K. Ozawa, 2008, Methods in molecular biology.

Crystal and Solution Structures of the Helicase-binding Domain of Escherichia coli Primase*

Guido Pintacuda, Gottfried Otting, Edvards Liepinsh, 2005, Journal of Biological Chemistry.

Sensitivity-enhanced double-TROSY experiment for simultaneous measurement of one-bond 15N-1H, 15N-13C' and two-bond 1H-13C' couplings.

G. Otting, M. Hoshino, 2004, Journal of magnetic resonance.

NMR structure of the WIF domain of the human Wnt-inhibitory factor-1.

G. Otting, E. Liepinsh, L. Patthy, 2006, Journal of molecular biology.

Water-protein NOEs: Optimized scheme for selective water excitation

G. Otting, E. Liepinsh, 1999, Journal of biomolecular NMR.

Selective excitation of intense solvent signals in the presence of radiation damping

G. Otting, E. Liepinsh, 1995, Journal of biomolecular NMR.

An α/β-HSQC-α/β Experiment for Spin-State Selective Editing of IS Cross Peaks

A. Annila, G. Otting, P. Andersson, 1998 .

An a/b-HSQC-a/b Experiment for Spin-State Selective Editing of IS Cross Peaks

A. Annila, G. Otting, P. Andersson, 1998 .

Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules

G. Otting, K. Wuethrich, 1989 .

Genetic Encoding of Cyanopyridylalanine for In‐Cell Protein Macrocyclization by the Nitrile–Aminothiol Click Reaction

G. Otting, T. Huber, C. Jackson, 2021, Angewandte Chemie.

Sensitivity enhancement in (HCA)CONH experiments

G. Otting, R. Folmer, 2000, Journal of biomolecular NMR.

Isolation and structure of a new galactolipid from oat seeds

M. Hamberg, G. Otting, E. Liepinsh, 1998, Lipids.

Site-selective tagging of proteins by pnictogen-mediated self-assembly.

G. Otting, T. Huber, Christoph Nitsche, 2017, Chemical communications.

Solution structure of a naturally-occurring zinc-peptide complex demonstrates that the N-terminal zinc-binding module of the Lasp-1 LIM domain is an independent folding unit.

K. Berndt, G. Otting, R. Sillard, 1996, Biochemistry.

Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) chelate.

G. Otting, G. Pintacuda, 2002, Journal of the American Chemical Society.

Inooh-Mediated Intergrown Heterojunctions for Enhanced Photocatalytic Performance: Assembly and Interfacial Charge Carrier Transferring

T. Frankcombe, X. Wen, G. Otting, 2022, SSRN Electronic Journal.

De Novo Discovery of Nonstandard Macrocyclic Peptides as Noncompetitive Inhibitors of the Zika Virus NS2B-NS3 Protease.

G. Otting, H. Suga, C. Klein, 2019, ACS medicinal chemistry letters.

NMR observation of individual molecules of hydration water bound to DNA duplexes: direct evidence for a spine of hydration water present in aqueous solution.

K. Wüthrich, G. Otting, E. Liepinsh, 1992, Nucleic Acids Research.

Pseudokontaktverschiebungen lokalisieren Eisen(III) in der zweikernigen Metallo‐β‐Laktamase IMP‐1

G. Otting, C. Jackson, P. Carr, 2014 .

Iron(III) located in the dinuclear metallo-β-lactamase IMP-1 by pseudocontact shifts.

G. Otting, C. Jackson, P. Carr, 2014, Angewandte Chemie.

Removal of zero-quantum coherence in protein NMR spectra using SESAM decoupling and suppression of decoupling sidebands.

J. Weigelt, G. Otting, W. Bermel, 1996, Journal of magnetic resonance. Series B.

Small Gd(III) Tags for Gd(III)-Gd(III) Distance Measurements in Proteins by EPR Spectroscopy.

G. Otting, D. Goldfarb, J. Swarbrick, 2018, Inorganic chemistry.

Overcoming artificial broadening in Gd(3+)-Gd(3+) distance distributions arising from dipolar pseudo-secular terms in DEER experiments.

G. Otting, V. Frydman, D. Goldfarb, 2016, Physical chemistry chemical physics : PCCP.

Protein Hydration Viewed by High‐Resolution NMR Spectroscopy: Implications for Magnetic Resonance Image Contrast

G. Otting, E. Liepinsh, 1995 .

Isolation and sequence‐specific DNA binding of the Antennapedia homeodomain.

K. Wüthrich, W. Gehring, M. Affolter, 1988, The EMBO journal.

N-Labelled proteins by cell-free protein synthesis. Strategies for high-throughput NMR studies of proteins and protein-ligand complexes.

N. Dixon, G. Otting, K. Ozawa, 2006, The FEBS journal.

POMA: A Complete Mathematica Implementation of the NMR Product-Operator Formalism

K. Wüthrich, P. Güntert, G. Otting, 1993 .

Conversion of an amide to a high-energy thioester by Staphylococcus aureus sortase A is powered by variable binding affinity for calcium

G. Otting, Jialiang Chen, Xiao Wang, 2018, Scientific Reports.

Phosphoserine for the generation of lanthanide-binding sites on proteins for paramagnetic nuclear magnetic resonance spectroscopy

G. Otting, M. Mahawaththa, Choy-Theng Loh, 2021 .

Phosphoserine for the generation of lanthanide binding sites on proteins for paramagnetic NMR

G. Otting, M. Mahawaththa, Choy-Theng Loh, 2020 .

The three‐dimensional NMR‐solution structure of the polypeptide fragment 195–286 of the LFB1/HNF1 transcription factor from rat liver comprises a nonclassical homeodomain.

K. Wüthrich, R. Cortese, G. Otting, 1993, The EMBO journal.

Luminescent Alkyne-Bearing Terbium(III) Complexes and Their Application to Bioorthogonal Protein Labeling.

G. Otting, L. Spiccia, G. Gasser, 2016, Inorganic chemistry.

Bound or free: interaction of the C-terminal domain of Escherichia coli single-stranded DNA-binding protein (SSB) with the tetrameric core of SSB.

N. Dixon, M. Vandevenne, G. Otting, 2014, Biochemistry.

Spectroscopic selection of distance measurements in a protein dimer with mixed nitroxide and Gd3+ spin labels.

G. Otting, T. Huber, D. Goldfarb, 2012, Physical chemistry chemical physics : PCCP.

Cell-free Protein Synthesis in an Autoinduction System for NMR Studies of Protein–Protein Interactions

S. Jergic, G. Otting, K. Ozawa, 2005, Journal of biomolecular NMR.

Rapid pulse length determination in high-resolution NMR.

G. Otting, Peter S. C. Wu, 2005, Journal of magnetic resonance.

Chemical Tagging with tert-Butyl and Trimethylsilyl Groups for Measuring Intermolecular Nuclear Overhauser Effects in a Large Protein-Ligand Complex.

G. Otting, L. Aurelio, B. Graham, 2017, Chemistry.

Ruthenium complexes of substituted hydrazine: new solution- and solid-state binding modes.

G. Otting, A. Willis, B. Messerle, 2008, Chemistry.

Genetic Encoding of para-Pentafluorosulfanyl Phenylalanine: A Highly Hydrophobic and Strongly Electronegative Group for Stable Protein Interactions.

N. Dixon, G. Otting, T. Huber, 2020, Journal of the American Chemical Society.

Random coil conformation of a Gly/Ala‐rich insert in IκBα excludes structural stabilization as the mechanism for protection against proteasomal degradation

G. Otting, M. Masucci, E. Liepinsh, 1998 .

Chapter 8 Use of high power spin-lock purge pulses in high resolution NMR spectroscopy

G. Otting, 1997 .

Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags

G. Otting, D. Goldfarb, A. Feintuch, 2015, Journal of Biomolecular NMR.

Structure restraints from heteronuclear pseudocontact shifts generated by lanthanide tags at two different sites

G. Otting, B. Graham, M. Szabó, 2017, Journal of Biomolecular NMR.

Selective 15N-labeling of the side-chain amide groups of asparagine and glutamine for applications in paramagnetic NMR spectroscopy

Y. Yang, G. Otting, X. Su, 2014, Journal of Biomolecular NMR.

Biosynthetically directed 2H labelling for stereospecific resonance assignments of glycine methylene groups

G. Otting, Karin V. Loscha, 2012, Journal of Biomolecular NMR.

Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O

G. Otting, Ruhu Qi, Choy-Theng Loh, 2011, Journal of biomolecular NMR.

Glutarate and N-acetyl-l-glutamate buffers for cell-free synthesis of selectively 15N-labelled proteins

G. Otting, K. Ozawa, Karin V. Loscha, 2009, Journal of biomolecular NMR.

1 Bound or Free : Interaction of the C-Terminal Domain of E . coli Single-Stranded DNA-Binding Protein ( SSB ) with the Tetrameric Core of SSB

N. Dixon, M. Vandevenne, G. Otting, 2018 .

Localising nuclear spins by pseudocontact shifts from a single tagging site

G. Otting, Stephen J. Butler, Elwy H. Abdelkader, 2022, Magnetic Resonance.

Supplementary material to "Localising individual atoms of tryptophan side chains in the metallo-β-lactamase IMP-1 by pseudocontact shifts from paramagnetic lanthanoid tags at multiple sites"

G. Otting, B. Graham, M. Szabó, 2021, Magnetic Resonance.

Measurement of small heteronuclear 1H15N coupling constants in 15N-labeled proteins by 3D HNNHAB-COSY

K. Wüthrich, G. Otting, K. Chary, 1991 .

Site-Specific Incorporation of Selenocysteine by Genetic Encoding as a Photocaged Unnatural Amino Acid.

G. Otting, T. Huber, B. Graham, 2018, Bioconjugate chemistry.

Paramagnetic Chemical Probes for Studying Biological Macromolecules

G. Otting, M. Ubbink, M. Overhand, 2022, Chemical reviews.

NMR structure of oxidized glutaredoxin 3 from Escherichia coli.

K. Berndt, G. Otting, A. Holmgren, 2000, Journal of molecular biology.

Clean TOCSY for proton spin system identification in macromolecules

Christian Griesinger, Richard R. Ernst, Gottfried Otting, 1988 .

Prospects for lanthanides in structural biology by NMR

Gottfried Otting, G. Otting, 2008, Journal of biomolecular NMR.

Proton exchange with internal water molecules in the protein BPTI in aqueous solution

G. Otting, E. Liepinsh, K. Wuethrich, 1991 .

Glutaredoxin-3 from Escherichia coli

K. Berndt, H. Jörnvall, T. Bergman, 1996, The Journal of Biological Chemistry.

Hydration of proteins. A comparison of experimental residence times of water molecules solvating the bovine pancreatic trypsin inhibitor with theoretical model calculations.

K Wüthrich, W F van Gunsteren, G Otting, 1993, Journal of molecular biology.

Heteronuclear filters in two-dimensional [1H, 1H]-NMR spectroscopy: combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions

K. Wüthrich, G. Otting, 1990, Quarterly Reviews of Biophysics.

Engineering of a bis-chelator motif into a protein α-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy.

G. Otting, T. Huber, X. Su, 2011, Chemical communications.

NMR structure determination of protein-ligand complexes by lanthanide labeling.

Guido Pintacuda, Gottfried Otting, G. Otting, 2007, Accounts of chemical research.

Protein Hydration Viewed by High-Resolution NMR Spectroscopy: Implications for Magnetic Resonance Image Contrast

G. Otting, E. Liepinsh, 1995 .

Gd³⁺ Spin Labeling for Measuring Distances in Biomacromolecules: Why and How?

G. Otting, D. Goldfarb, A. Feintuch, 2015, Methods in enzymology.

Backbone assignment of fully protonated solid proteins by 1H detection and ultrafast magic-angle-spinning NMR spectroscopy.

Lyndon Emsley, Michele Felletti, Anne Lesage, 2012, Angewandte Chemie.

Paramagnetic labelling of proteins and oligonucleotides for NMR

G. Otting, X. Su, Xuncheng Su, 2010, Journal of biomolecular NMR.

RIDME distance measurements using Gd(iii) tags with a narrow central transition.

G. Otting, V. Frydman, D. Goldfarb, 2016, Physical chemistry chemical physics : PCCP.

Gadolinium(III) spin labels for high-sensitivity distance measurements in transmembrane helices.

G. Otting, T. Huber, V. Frydman, 2013, Angewandte Chemie.

W-band orientation selective DEER measurements on a Gd3+/nitroxide mixed-labeled protein dimer with a dual mode cavity.

G. Otting, T. Huber, Nurit Manukovsky, 2013, Journal of magnetic resonance.

Gadolinium tagging for high-precision measurements of 6 nm distances in protein assemblies by EPR.

Thomas Huber, Gottfried Otting, Hiromasa Yagi, 2011, Journal of the American Chemical Society.

Nanometer-scale distance measurements in proteins using Gd3+ spin labeling.

S. Jergic, N. Dixon, G. Otting, 2010, Journal of the American Chemical Society.

NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism.

K. Berndt, G. Otting, A. Holmgren, 1999, Journal of molecular biology.

Multiple-site labeling of proteins with unnatural amino acids.

Thomas Huber, Gottfried Otting, G. Otting, 2012, Angewandte Chemie.

Secondary structure determination for the Antennapedia homeodomain by nuclear magnetic resonance and evidence for a helix‐turn‐helix motif.

K. Wüthrich, W. Gehring, M. Affolter, 1988, The EMBO journal.

A heteronuclear three-dimensional NMR experiment for measurements of small heteronuclear coupling constants in biological macromolecules

G. Wider, D. Neri, G. Otting, 1989 .

Improved Spectral Resolution in 1H NMR Spectroscopy by Homonuclear Semiselective Shaped Pulse Decoupling during Acquisition

G. Otting, A. Hammarstroem, G. Otting, 1994 .

1H-Detected INEPT-INADEQUATE at Natural 13C Abundance

J. Weigelt, G. Otting, 1995 .

Long-Range HSQC with Spin-Lock Purge Pulses for the Observation of Heteronuclear Correlations with1H Detection and Lowt1Noise

G. Otting, A. Koskinen, S. Mattila, 1995 .

How reliable are pseudocontact shifts induced in proteins and ligands by mobile paramagnetic metal tags? A modelling study

G. Otting, D. Shishmarev, 2013, Journal of Biomolecular NMR.

How reliable are pseudocontact shifts induced in proteins and ligands by mobile paramagnetic metal tags? A modelling study

G. Otting, Dmitry Shishmarev, D. Shishmarev, 2013, Journal of Biomolecular NMR.

A systematic study of labelling an α-helix in a protein with a lanthanide using IDA-SH or NTA-SH tags

G. Otting, A. Maleckis, H. Yagi, 2013, Journal of biomolecular NMR.

Lanthanide tags for site-specific ligation to an unnatural amino acid and generation of pseudocontact shifts in proteins.

Thomas Huber, Gottfried Otting, G. Otting, 2013, Bioconjugate chemistry.

A systematic study of labelling an α-helix in a protein with a lanthanide using IDA-SH or NTA-SH tags

G. Otting, A. Maleckis, H. Yagi, 2012, Journal of Biomolecular NMR.

3-Mercapto-2,6-pyridinedicarboxylic acid: a small lanthanide-binding tag for protein studies by NMR spectroscopy.

G. Otting, T. Huber, X. Su, 2010, Chemistry.

Structure of the θ Subunit of Escherichia coli DNA Polymerase III in Complex with the ε Subunit

S. Hamdan, N. Dixon, G. Otting, 2006, Journal of bacteriology.

1H-Detected Multinuclear NMR Experiments for the Measurement of Small Heteronuclear Coupling Constants in Transition Metal Complexes

G. Otting, B. Messerle, L. Soler, 1997 .

Precise vicinal coupling constants3JHNα in proteins from nonlinear fits of J-modulated [15N,1H]-COSY experiments

M. Billeter, K. Wüthrich, D. Neri, 1992 .

New nuclear magnetic resonance experiment for measurements of the vicinal coupling constants 3JHN.alpha. in proteins

D. Neri, G. Otting, K. Wuethrich, 1990 .

Spin-state selection filters for the measurement of heteronuclear one-bond coupling constants

J. Weigelt, G. Otting, P. Andersson, 1998, Journal of biomolecular NMR.

Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets

Kurt Wüthrich, Thomas Szyperski, Peter Güntert, 1992 .

13C-Relayed 13C HSQC at natural isotopic abundance

J. Weigelt, G. Otting, 1995 .

Efficient purging scheme for proton-detected heteronuclear two-dimensional NMR

K. Wüthrich, G. Otting, 1988 .

Heteronuclear correlation experiments for the determination of one-bond coupling constants

G. Otting, E. Liepinsh, M. Sunnerhagen, 1998, Journal of biomolecular NMR.

Protein structure determination from pseudocontact shifts using ROSETTA.

David Baker, Thomas Huber, Gottfried Otting, 2012, Journal of molecular biology.

Selective Distance Measurements Using Triple Spin Labeling with Gd3+, Mn2+, and a Nitroxide.

G. Otting, D. Goldfarb, A. Feintuch, 2017, The journal of physical chemistry letters.

Protein conformation by EPR spectroscopy using gadolinium tags clicked to genetically encoded p-azido-L-phenylalanine.

G. Otting, D. Goldfarb, A. Feintuch, 2015, Chemical communications.

Nanometer-range distance measurement in a protein using Mn 2+ tags

G. Otting, T. Huber, D. Goldfarb, 2012 .

Through-Space Scalar 19F-19F Couplings between Fluorinated Noncanonical Amino Acids for the Detection of Specific Contacts in Proteins.

G. Otting, T. Huber, C. Jackson, 2021, Journal of the American Chemical Society.

Protein–DNA contacts in the structure of a homeodomain–DNA complex determined by nuclear magnetic resonance spectroscopy in solution.

K Wüthrich, G Otting, Y Q Qian, 1990, The EMBO journal.

COMMUNICATIONS: Extended Heteronuclear Editing of 2D 1H NMR Spectra of Isotope-Labeled Proteins, Using the X(ω1, ω2) Double Half Filter

K. Wüthrich, G. Otting, 1995 .

Extended heteronuclear editing of 2D 1H NMR spectra of isotope-labeled proteins, using the X(ω1, ω2) double half filter

K. Wüthrich, G. Otting, 1989 .

Editing of 2D 1H NMR spectra using X half-filters. combined use with residue-selective 15N labeling of proteins

K. Wüthrich, G. Wagner, H. Senn, 1986 .

A New Gd(3+) Spin Label for Gd(3+)-Gd(3+) Distance Measurements in Proteins Produces Narrow Distance Distributions.

G. Otting, D. Goldfarb, J. Swarbrick, 2015, The journal of physical chemistry letters.

DOTA-amide lanthanide tag for reliable generation of pseudocontact shifts in protein NMR spectra.

Thomas Huber, Guido Pintacuda, Gottfried Otting, 2011, Bioconjugate chemistry.

NMR structure of the death domain of the p 75 neurotrophin receptor affinity binding sites ( Hempstead et al . , 1991 ; Mahadeo

G. Otting, E. Liepinsh, L. Ilag, 1997 .

Double-Arm Lanthanide Tags Deliver Narrow Gd3+ -Gd3+ Distance Distributions in Double Electron-Electron Resonance (DEER) Measurements.

G. Otting, T. Huber, D. Goldfarb, 2017, Chemistry.

New Lanthanide Tag for the Generation of Pseudocontact Shifts in DNA by Site-Specific Ligation to a Phosphorothioate Group.

G. Otting, J. Swarbrick, M. Dennis, 2017, Bioconjugate chemistry.

Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex.

K Wüthrich, G Otting, Y Q Qian, 1993, Journal of molecular biology.

Site-selective generation of lanthanoid binding sites on proteins using 4-fluoro-2,6-dicyanopyridine

G. Otting, T. Huber, D. Goldfarb, 2022, Magnetic Resonance.

Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme

G. Otting, C. Jackson, D. Goldfarb, 2020, Nature Communications.

Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags

G. Otting, D. Goldfarb, A. Feintuch, 2016, Journal of biomolecular NMR.

NMR structure of the death domain of the p75 neurotrophin receptor

G. Otting, E. Liepinsh, L. Ilag, 1997, The EMBO journal.

Role of charged and hydrophobic residues in the oligomerization of the PYRIN domain of ASC.

G. Otting, E. Liepinsh, J. Sagara, 2005, Biochemistry.

The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition.

E. Dahl, E. Staub, G. Otting, 2003, Journal of molecular biology.

Modulation of the distance dependence of paramagnetic relaxation enhancements by CSA x DSA cross-correlation.

G. Otting, G. Pintacuda, A. Kaikkonen, 2004, Journal of magnetic resonance.

NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins

K. Wüthrich, G. Otting, E. Liepinsh, 1992, Journal of biomolecular NMR.

NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer.

J Weigelt, G Otting, N. Dixon, 1999, Structure.

NMR structure of the LCCL domain and implications for DFNA9 deafness disorder

J. Weigelt, G. Otting, E. Liepinsh, 2001, The EMBO journal.

Proton exchange rates from amino acid side chains— implications for image contrast

Gottfried Otting, Edvards Liepinsh, G. Otting, 1996, Magnetic resonance in medicine.

Selection of a peptide ligand to the p75 neurotrophin receptor death domain and determination of its binding sites by NMR.

G. Otting, E. Liepinsh, L. Ilag, 1999, Biochemical and biophysical research communications.

Protein hydration in aqueous solution.

K. Wüthrich, G. Otting, E. Liepinsh, 1991, Science.

Mutations in the COCH gene are a frequent cause of autosomal dominant progressive cochleo-vestibular dysfunction, but not of Meniere's disease

G. Otting, E. Fransen, L. Patthy, 2003, European Journal of Human Genetics.

3D Structure Determination of an Unstable Transient Enzyme Intermediate by Paramagnetic NMR Spectroscopy.

G. Otting, Feng Yang, Jialiang Chen, 2016, Angewandte Chemie.

Main protease mutants of SARS-CoV-2 variants remain susceptible to nirmatrelvir

G. Otting, Christoph Nitsche, K. Ekanayake, 2021, bioRxiv.

Memory T cell RNA rearrangement programmed by heterogeneous nuclear ribonucleoprotein hnRNPLL.

D. Zak, A. Aderem, B. Marzolf, 2008, Immunity.

Solution structure of a hydrophobic analogue of the winter flounder antifreeze protein.

J. Mackay, G. Otting, E. Liepinsh, 2002, European journal of biochemistry.

Stabilization of native protein fold by intein-mediated covalent cyclization.

Phil Attard, Gottfried Otting, N. K. Williams, 2005, Journal of molecular biology.

A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader

N. Dixon, G. Otting, E. Liepinsh, 2009, Nucleic acids research.

The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: Comparison with prokaryotic repressors

W. J. Gehring, M. Billeter, K. Wüthrich, 1989, Cell.

The structure of the homeodomain and its functional implications.

M. Billeter, K. Wüthrich, W. Gehring, 1990, Trends in genetics : TIG.

Protein NMR using paramagnetic ions.

G. Otting, 2010, Annual review of biophysics.

Supporting Information for : Identification of Protein Surfaces by NMR Measurements with a Paramagnetic Gd ( III ) Chelate

G. Otting, G. Pintacuda, 2001 .

Expression, purification, crystallization, and NMR studies of the helicase interaction domain of Escherichia coli DnaG primase.

N. Dixon, G. Otting, M. Wilce, 2004, Protein expression and purification.

- 1-Chaperonin-Encapsulation of Proteins for NMR

Katsumi, N. Dixon, G. Otting, 2019 .

Chaperonin-encapsulation of proteins for NMR.

N. Dixon, G. Otting, K. Matsuzaki, 2010, Biochimica et biophysica acta.

Structure of the RTP–DNA complex and the mechanism of polar replication fork arrest

J. Wilce, G. Otting, J. Vivian, 2001, Nature Structural Biology.

Specificity of Urea Binding to Proteins

Gottfried Otting, Edvards Liepinsh, G. Otting, 1994 .

NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains.

B. Joris, G. Otting, E. Liepinsh, 2003, Journal of molecular biology.

Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III.

D. Ollis, S. Hamdan, N. Dixon, 2000, Journal of structural biology.

Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F)

G. Otting, E. Liepinsh, M. Kitamura, 1997, Nature Structural Biology.

Common ancestor of serine proteases and flavin-binding domains

G. Otting, E. Liepinsh, M. Kitamura, 1998, Nature Structural Biology.

Hydration Studies of Biological Macromolecules by Intermolecular Water-Solute NOEs

G. Otting, 2002 .

NMR studies of water bound to biological molecules

Gottfried Otting, G. Otting, 1997 .

NMR identification of hydrophobic cavities with ow water occupancies in protein structures using small gas molecules

G. Otting, B. Halle, E. Liepinsh, 1997, Nature Structural Biology.

Protein dynamics studied by rotating frame 15N spin relaxation times

T Szyperski, P Luginbühl, K Wüthrich, 1993, Journal of biomolecular NMR.

Translational incorporation of L‐3,4‐dihydroxyphenylalanine into proteins

R. Dean, N. Dixon, G. Otting, 2005, The FEBS journal.

Dynamics of protein and peptide hydration.

G. Otting, B. Halle, E. Liepinsh, 2004, Journal of the American Chemical Society.

Challenges of short substrate analogues as SARS-CoV-2 main protease inhibitors

G. Otting, Christoph Nitsche, M. Mahawaththa, 2021, Bioorganic & Medicinal Chemistry Letters.

Experimental NMR techniques for studies of protein-ligand interactions

G. Otting, 1993 .

Engineering [Ln(DPA)3]3− binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions

G. Otting, T. Huber, Mitchell Stanton-Cook, 2011, Journal of biomolecular NMR.

Analysis of the solution conformations of T4 lysozyme by paramagnetic NMR spectroscopy.

Y. Yang, G. Otting, T. Huber, 2016, Physical chemistry chemical physics : PCCP.

Efficient χ-tensor determination and NH assignment of paramagnetic proteins

N. Dixon, G. Otting, T. Huber, 2006, Journal of biomolecular NMR.

Weak alignment of paramagnetic proteins warrants correction for residual CSA effects in measurements of pseudocontact shifts.

Guido Pintacuda, Gottfried Otting, Nicholas E Dixon, 2005, Journal of the American Chemical Society.

Mutant T4 DNA polymerase for easy cloning and mutagenesis

G. Otting, Ruhu Qi, 2019, PloS one.

In Vivo Protein Cyclization Promoted by a Circularly Permuted Synechocystis sp. PCC6803 DnaB Mini-intein*

Nicholas E. Dixon, Paul M. G. Curmi, Gottfried Otting, 2002, The Journal of Biological Chemistry.

NMR experiments for the sign determination of homonuclear scalar and residual dipolar couplings

G. Otting, M. Levitt, A. Moshref, 2000, Journal of biomolecular NMR.

Improving a natural enzyme activity through incorporation of unnatural amino acids.

Colin J Jackson, Gottfried Otting, Gerhard Schenk, 2011, Journal of the American Chemical Society.

Solution structure of Domains IVa and V of the τ subunit of Escherichia coli DNA polymerase III and interaction with the α subunit

S. Jergic, N. Dixon, G. Otting, 2007, Nucleic acids research.

Solution structure of Domains IVa and V of the tau subunit of Escherichia coli DNA polymerase III and interaction with the alpha subunit

S. Jergic, N. Dixon, G. Otting, 2007 .

Structure determination of the Antp (C39----S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA.

K. Wüthrich, P. Güntert, W. Gehring, 1991, Journal of molecular biology.

Determination of the three-dimensional structure of theAntennapedia homeodomain fromDrosophila in solution by1H nuclear magnetic resonance spectroscopy

Gottfried Otting, Walter J. Gehring, Martin Billeter, 1990 .

Thiol-ene reaction: a versatile tool in site-specific labelling of proteins with chemically inert tags for paramagnetic NMR.

Y. Yang, G. Otting, X. Su, 2012, Chemical communications.

Binding of low molecular weight inhibitors promotes large conformational changes in the dengue virus NS2B-NS3 protease: fold analysis by pseudocontact shifts.

G. Otting, T. Huber, K. Ozawa, 2011, Journal of the American Chemical Society.

Intramolecular binding mode of the C-terminus of Escherichia coli single-stranded DNA binding protein determined by nuclear magnetic resonance spectroscopy

N. Dixon, G. Otting, T. Huber, 2013, Nucleic acids research.

Monomeric solution structure of the helicase‐binding domain of Escherichia coli DnaG primase

Gottfried Otting, Nicholas E Dixon, N. Dixon, 2006, The FEBS journal.

The unstructured C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunit

N. K. Williams, S. Hamdan, S. Jergic, 2017 .

Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, ε, θ and β reveals a highly flexible arrangement of the proofreading domain

Thomas Huber, Nan Li, Nicholas E. Dixon, 2013, Nucleic acids research.

The unstructured C-terminus of the τ subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the α subunit

N. K. Williams, S. Hamdan, S. Jergic, 2007, Nucleic acids research.

Solvent suppression using a spin lock in 2D and 3D NMR spectroscopy with H2O solutions

G. Wider, K. Wüthrich, G. Otting, 1989 .

Erratum to “NMR studies of water bound to biological molecules”

G. Otting, 1998 .

Disulfide bond isomerization in BPTI and BPTI(G36S): an NMR study of correlated mobility in proteins.

K. Wüthrich, G. Otting, E. Liepinsh, 1993, Biochemistry.

Letter to the Editor: Backbone 1H, 13C and 15N resonance assignment of the N-terminal 24 kDa fragment of the gyrase B subunit from E. coli

E. Domenici, J. Weigelt, G. Otting, 2002, Journal of Biomolecular NMR.

Backbone NMR Assignments and Secondary Structure of the N-terminal Domain of DnaB Helicase from E. Coli

N. Dixon, J. Weigelt, G. Otting, 1998, Journal of biomolecular NMR.

Precise limits of the N-terminal domain of DnaB helicase determined by NMR spectroscopy.

N. Dixon, J. Weigelt, G. Otting, 1997, Biochemical and biophysical research communications.

The mechanism of the anaerobic Escherichia coli ribonucleotide reductase investigated with nuclear magnetic resonance spectroscopy.

G. Otting, M. Fontecave, E. Liepinsh, 1995, Biochemical and biophysical research communications.

Suppression of zero-quantum coherence in NOESY and soft NOESY

K. Wüthrich, G. Otting, L. Orbons, 1990 .

Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor (1 to 76) in solution and comparison with the DNA-binding domain of the 434 repressor.

K. Wüthrich, G. Otting, P. Sevilla-Sierra, 1994, Journal of molecular biology.

Support of1H NMR assignments in proteins by biosynthetically directed fractional13C-labeling

K. Wüthrich, T. Szyperski, D. Neri, 1992 .

Support of 1H NMR assignments in proteins by biosynthetically directed fractional 13C-labeling.

K. Wüthrich, T. Szyperski, D. Neri, 1992, Journal of biomolecular NMR.

Structure determination of protein-ligand complexes by transferred paramagnetic shifts.

N. Dixon, G. Otting, Michael John, 2006, Journal of the American Chemical Society.

Selective 15N-labeling of the side-chain amide groups of asparagine and glutamine for applications in paramagnetic NMR spectroscopy

Y. Yang, G. Otting, X. Su, 2014, Journal of biomolecular NMR.

Sequence-specific 1H-NMR assignments and determination of the secondary structure in aqueous solution of the cardiotoxins CTXIIa and CTXIIb from Naja mossambica mossambica.

K. Wüthrich, G. Otting, P. Bougis, 1987, European journal of biochemistry.

Short-range ENDOR distance measurements between Gd(III) and trifluoromethyl labels in proteins.

G. Otting, T. Huber, A. Godt, 2022, Physical chemistry chemical physics : PCCP.

Three-dimensional protein fold determination from backbone amide pseudocontact shifts generated by lanthanide tags at multiple sites.

Thomas Huber, Gottfried Otting, Kala Bharath Pilla, 2013, Structure.

Generation of pseudocontact shifts in protein NMR spectra with a genetically encoded cobalt(II)-binding amino acid.

G. Otting, T. Huber, K. Ozawa, 2011, Angewandte Chemie.

A dipicolinic acid tag for rigid lanthanide tagging of proteins and paramagnetic NMR spectroscopy.

G. Otting, T. Huber, C. Schmitz, 2008, Journal of the American Chemical Society.

NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin.

G. Otting, H. Ponstingl, 1997, European journal of biochemistry.

NT*-HRV3CP: an optimized construct of human rhinovirus 14 3C protease for high-yield expression and fast affinity-tag cleavage.

G. Otting, Elwy H. Abdelkader, 2020, Journal of biotechnology.

A fluorescence quenching assay to discriminate between specific and nonspecific inhibitors of dengue virus protease.

A. Caflisch, G. Otting, D. Wen, 2009, Analytical biochemistry.

Zero-quantum suppression in NOESY and experiments with a z filter

G. Otting, 1990 .

Probing Ligand Binding Sites on Large Proteins by Nuclear Magnetic Resonance Spectroscopy of Genetically Encoded Non-Canonical Amino Acids.

G. Otting, T. Huber, R. Payne, 2023, Journal of medicinal chemistry.

Dynamic Liquid State NMR and IR Study of Tautomerism and Conformations of Tetraphenyloxalamidine, a Novel Small Intramolecular Double Hydrogen Transfer System

G. Otting, H. Rumpel, H. Limbach, 1986 .

Edvards Liepinsh, MaÂ

J. Weigelt, G. Otting, E. Liepinsh, 2022 .

Biosynthetically directed 2H labelling for stereospecific resonance assignments of glycine methylene groups

G. Otting, Karin V. Loscha, 2012, Journal of Biomolecular NMR.

Flaviviral protease inhibitors identified by fragment-based library docking into a structure generated by molecular dynamics.

Amedeo Caflisch, Danzhi Huang, Gottfried Otting, 2009, Journal of medicinal chemistry.

1 Identification of lead-like and non-lead-like inhibitors for dengue virus NS 2 B / NS 3 protease by tryptophan fluorescence

A. Caflisch, G. Otting, D. Wen, 2009 .

Lanthanide-binding peptides for NMR measurements of residual dipolar couplings and paramagnetic effects from multiple angles.

G. Otting, T. Huber, X. Su, 2008, Journal of the American Chemical Society.

Genetic Encoding of N6-(((Trimethylsilyl)methoxy)carbonyl)-l-lysine for NMR Studies of Protein-Protein and Protein-Ligand Interactions.

G. Otting, T. Huber, L. A. Adams, 2021, Journal of the American Chemical Society.

Pseudocontact Shift-Driven Iterative Resampling for 3D Structure Determinations of Large Proteins.

Thomas Huber, Gottfried Otting, Kala Bharath Pilla, 2016, Journal of molecular biology.

Genetically encoded amino acids with tert-butyl and trimethylsilyl groups for site-selective studies of proteins by NMR spectroscopy

G. Otting, B. Graham, L. A. Adams, 2018, Journal of biomolecular NMR.

Trimethylsilyl tag for probing protein–ligand interactions by NMR

G. Otting, K. Zangger, B. Graham, 2018, Journal of biomolecular NMR.

Trimethylsilyl tag for probing protein–ligand interactions by NMR

G. Otting, K. Zangger, B. Graham, 2018, Journal of Biomolecular NMR.

Genetically encoded amino acids with tert-butyl and trimethylsilyl groups for site-selective studies of proteins by NMR spectroscopy

G. Otting, B. Graham, L. A. Adams, 2017, Journal of Biomolecular NMR.

Cell-free synthesis and combinatorial selective 15N-labeling of the cytotoxic protein amoebapore A from Entamoeba histolytica.

N. Dixon, M. Leippe, G. Otting, 2009, Protein expression and purification.

Measurement of dissociation constants of high-molecular weight protein–protein complexes by transferred 15N-relaxation

S. Jergic, N. Dixon, G. Otting, 2007, Journal of biomolecular NMR.

Ring opening of benzo[a]pyrene in the germ-free rat is a novel pathway for formation of potentially genotoxic metabolites.

J. Gustafsson, G. Otting, J. Bergman, 2000, Biochemistry.

Rapid Measurement of Scalar Three-bond 1HN-1Hα spin coupling constants in 15N-labelled proteins

G. Otting, H. Ponstingl, 1998 .

SWET for Secure Water Suppression on Probes with High Quality Factor

G. Otting, Peter S. C. Wu, 2005, Journal of biomolecular NMR.

NMR Structure of the Netrin-like Domain (NTR) of Human Type I Procollagen C-Proteinase Enhancer Defines Structural Consensus of NTR Domains and Assesses Potential Proteinase Inhibitory Activity and Ligand Binding*

G. Otting, E. Liepinsh, L. Patthy, 2003, Journal of Biological Chemistry.

Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.

M. Ingelman-Sundberg, G. Otting, E. Liepinsh, 2001, Structure.

Sensitive 1H-31P correlations with 5′ methylene protons of DNA via homonuclear double-quantum coherence

G. Otting, A. Kaikkonen, 2001, Journal of biomolecular NMR.

Amino-acid Type Identification in 15N-HSQC Spectra by Combinatorial Selective 15N-labelling

Gottfried Otting, Slobodan Jergic, Nicholas E Dixon, 2006, Journal of biomolecular NMR.

Fast structure-based assignment of 15N HSQC spectra of selectively 15N-labeled paramagnetic proteins.

Thomas Huber, Guido Pintacuda, Gottfried Otting, 2004, Journal of the American Chemical Society.

Fragment-Based Discovery of Inhibitors of the Bacterial DnaG-SSB Interaction

N. Dixon, G. Otting, Zhi-Qiang Xu, 2018, Antibiotics.

Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK‐lysin

G. Otting, A. Karshikoff, M. Miteva, 1999, FEBS letters.

Lanthanide labeling offers fast NMR approach to 3D structure determinations of protein-protein complexes.

Guido Pintacuda, Gottfried Otting, Nicholas E Dixon, 2006, Journal of the American Chemical Society.

DEER experiments reveal fundamental differences between calmodulin complexes with IQ and MARCKS peptides in solution.

G. Otting, G. Jeschke, S. Bhattacharya, 2022, Structure.

3D protein structure determination using pseudocontact shifts of backbone amide protons generated by double-histidine Co2+-binding motifs at multiple sites.

G. Otting, T. Huber, Alireza Bahramzadeh, 2019, Biochemistry.

O-tert-Butyltyrosine, an NMR tag for high-molecular-weight systems and measurements of submicromolar ligand binding affinities.

G. Otting, T. Huber, Wan-Na Chen, 2015, Journal of the American Chemical Society.

Tunable paramagnetic relaxation enhancements by [Gd(DPA)3]3− for protein structure analysis

G. Otting, T. Huber, X. Su, 2010, Journal of biomolecular NMR.

[Ln(DPA)(3)](3-) is a convenient paramagnetic shift reagent for protein NMR studies.

G. Otting, X. Su, Karin V. Loscha, 2009, Journal of the American Chemical Society.

Site‐Specific Labelling of Proteins with a Rigid Lanthanide‐Binding Tag

N. Dixon, G. Otting, T. Huber, 2006, Chembiochem : a European journal of chemical biology.

Optimization of an Escherichia coli system for cell-free synthesis of selectively N-labelled proteins for rapid analysis by NMR spectroscopy.

N. Dixon, G. Otting, P. Schaeffer, 2004, European journal of biochemistry.

NMR analysis of in vitro‐synthesized proteins without purification: a high‐throughput approach

N. Dixon, G. Otting, K. Ozawa, 2002, FEBS letters.

Sequence-and stereospecific assignment of methyl groups using paramagnetic lanthanides

N. Dixon, G. Otting, T. Huber, 2007 .

Capturing Conformational States in Proteins Using Sparse Paramagnetic NMR Data

G. Otting, T. Huber, K. B. Pilla, 2015, PloS one.

Angular dependence of dipole-dipole-Curie-spin cross-correlation effects in high-spin and low-spin paramagnetic myoglobin**

G. Otting, G. Pintacuda, N. Müller, 2003, Journal of biomolecular NMR.

Hydration of DNA in aqueous solution: NMR evidence for a kinetic destabilization of the minor groove hydration of d-(TTAA)2 versus d-(AATT)2 segments.

G. Otting, E. Liepinsh, W. Leupin, 1994, Nucleic Acids Research.

Protein hydration studied with homonuclear 3D1H NMR experiments

K Wüthrich, G Otting, K. Wüthrich, 1991, Journal of biomolecular NMR.

Water molecules in DNA recognition I: hydration lifetimes of trp operator DNA in solution measured by NMR spectroscopy.

G. Otting, J. Carey, B. Halle, 1998, Journal of molecular biology.

Hydrophobic interactions in a cyanobacterial plastocyanin-cytochrome f complex.

G. Otting, P. B. Crowley, M. Ubbink, 2001, Journal of the American Chemical Society.

Solution structure of the R3H domain from human Smubp-2.

Gottfried Otting, Edvards Liepinsh, G. Otting, 2003, Journal of molecular biology.

NMR Structure Determination of ProteinLigand Complexes by Lanthanide Labeling

G. Otting, Michael John, X. Su, 2007 .

A Probehead with Switchable Quality Factor. Suppression of Radiation Damping

C. Anklin, G. Otting, F. Laukien, 1995 .

15N‐Labelled proteins by cell‐free protein synthesis

Nicholas E. Dixon, Gottfried Otting, N. Dixon, 2006 .

High-yield cell-free protein synthesis for site-specific incorporation of unnatural amino acids at two sites.

N. Dixon, G. Otting, K. Ozawa, 2012, Biochemical and biophysical research communications.

Protein Structure Determination by Assembling Super-Secondary Structure Motifs Using Pseudocontact Shifts.

Thomas Huber, Gottfried Otting, Kala Bharath Pilla, 2017, Structure.

Resource Protein Structure Determi nation by Assembling Super-Secondary Structure Motifs Using Pseudocontact Shifts Graphical

G. Otting, T. Huber, K. B. Pilla, 2017 .

Using Paramagnetism to Slow Down Nuclear Relaxation in Protein NMR.

G. Otting, I. Kuprov, Choy-Theng Loh, 2016, The journal of physical chemistry letters.

φ Angle Restraints in Protein Backbones from Dipole−Dipole Cross-Correlation between1HN−15N and1HN−1HαVectors

G. Otting, P. B. Crowley, M. Ubbink, 2000 .

Cell-free synthesis of proteins with selectively 13C-labelled methyl groups from inexpensive precursors

G. Otting, T. Huber, Damian van Raad, 2023, Magnetic Resonance.

The proofreading exonuclease subunit ε of Escherichia coli DNA polymerase III is tethered to the polymerase subunit α via a flexible linker

S. Jergic, N. Dixon, G. Otting, 2008, Nucleic acids research.

Nuclear magnetic resonance spectroscopy of a DNA complex with the uniformly 13C-labeled Antennapedia homeodomain and structure determination of the DNA-bound homeodomain.

K Wüthrich, G Otting, Y Q Qian, 1993, Journal of molecular biology.

Determination of the Three-dimensional Structure of the Antennapedia Homeodomain from Drosophila in Solution by 1H Nuclear Magnetic Resonance Spectroscopy

Kurt Wüthrich, Gottfried Otting, Walter Gehring, 1993 .

Polypeptide hydration in mixed solvents at low temperatures

Gottfried Otting, Edvards Liepinsh, G. Otting, 1992 .

Assignment of paramagnetic 15N-HSQC spectra by heteronuclear exchange spectroscopy

N. Dixon, G. Otting, Michael John, 2006, Journal of biomolecular NMR.

Protein Structure and Interactions by Combined Use of Sequential NMR Assignments and Isotope Labeling.

H. Senn, G. Otting, K. Wuethrich, 1987 .

1H And 13C NMR chemical shifts of the diastereotopic methyl groups of valyl and leucyl residues in peptides and proteins

K. Wüthrich, D. Neri, G. Otting, 1990 .

Two Histidines in an α-Helix: A Rigid Co2+ -Binding Motif for PCS Measurements by NMR Spectroscopy.

G. Otting, T. Huber, Hailun Jiang, 2018, Angewandte Chemie.

Using tert-Butyl Groups in a Ligand To Identify Its Binding Site on a Protein.

G. Otting, Wan-Na Chen, 2018, ACS medicinal chemistry letters.

Biocompatible Macrocyclization between Cysteine and 2-Cyanopyridine Generates Stable Peptide Inhibitors.

G. Otting, T. Huber, D. Luo, 2019, Organic letters.

Backbone 1H, 13C and 15N resonance assignment of the N-terminal 24 kDa fragment of the gyrase B subunit from E. coli.

E. Domenici, J. Weigelt, G. Otting, 2002, Journal of Biomolecular NMR.

Strategies for high-throughput NMR studies of proteins and protein-ligand complexes

N. Dixon, G. Otting, K. Ozawa, 2006 .

NMR detection of protein 15N spins near paramagnetic lanthanide ions.

N. Dixon, G. Otting, Michael John, 2007, Journal of the American Chemical Society.

Improved spectral resolution of [13C,1H]-HSQC spectra of aromatic amino acid residues in proteins produced by cell-free synthesis from inexpensive 13C-labelled precursors

G. Otting, T. Huber, Damian van Raad, 2023, Journal of Biomolecular NMR.

NMR studies of ligand binding.

G. Otting, Christoph Nitsche, 2018, Current opinion in structural biology.

Structural basis for 5'-end-specific recognition of single-stranded DNA by the R3H domain from human Sμbp-2.

Kristaps Jaudzems, Xinying Jia, Hiromasa Yagi, 2012, Journal of molecular biology.

Solution Structure of the R 3 H Domain from Human S m bp-2

G. Otting, E. Liepinsh, A. Leonchiks, 2003 .

Letter to the Editor: NMR structure of human coactosin-like protein

G. Otting, E. Liepinsh, B. Samuelsson, 2004 .

Second Kunitz-type protease inhibitor domain of the human WFIKKN1 protein

G. Otting, E. Liepinsh, L. Patthy, 2006, Journal of biomolecular NMR.

Synthesis of 13C/19F/2H labeled indoles for use as tryptophan precursors for protein NMR spectroscopy.

G. Otting, A. Maleckis, Iresha D. Herath, 2021, Organic & biomolecular chemistry.

Direct NMR observation of the Cys‐14 thiol proton of reduced Escherichia coli glutaredoxin‐3 supports the presence of an active site thiol‐thiolate hydrogen bond

K. Berndt, G. Otting, A. Holmgren, 1999, FEBS letters.

Flaviviral protease inhibitors identified by fragment-based library docking into a structure generated by molecular dynamics.

A. Caflisch, G. Otting, Dariusz Ekonomiuk, 2009, Journal of medicinal chemistry.

Backbone assignment of fully protonated solid proteins by 1H detection and ultrafast magic-angle-spinning NMR spectroscopy.

N. Dixon, G. Otting, A. Park, 2012, Angewandte Chemie.

Luminescent Alkyne-Bearing Terbium(III) Complexes and Their Application to Bioorthogonal Protein Labeling.

G. Otting, L. Spiccia, G. Gasser, 2016, Inorganic chemistry.

In situ deprotection and incorporation of unnatural amino acids during cell-free protein synthesis.

J. Oakeshott, G. Otting, Stéphanie Lesturgez, 2013, Chemistry.

NMR structure of the WIF domain of the human Wnt-inhibitory factor-1.

G. Otting, E. Liepinsh, L. Patthy, 2006, Journal of Molecular Biology.

Application of 13C(ω1)‐half‐filtered [1H,1H]‐NOESY for studies of a complex formed between DNA and a 13C‐labeled minor‐groove‐binding drug

K. Wüthrich, G. Otting, H. Amacker, 1990, FEBS letters.

Discovery of Antiviral Cyclic Peptides Targeting the Main Protease of SARS-CoV-2 via mRNA Display

G. Otting, C. Jackson, R. Payne, 2021, bioRxiv.

Lanthanide tags for site-specific ligation to an unnatural amino acid and generation of pseudocontact shifts in proteins.

G. Otting, T. Huber, K. Ozawa, 2013, Bioconjugate chemistry.

Chaperonin-encapsulation of proteins for NMR.

N. Dixon, G. Otting, K. Matsuzaki, 2010, Biochimica et Biophysica Acta.

3D Structure of the Transient Intermediate of the Enzyme–Substrate Complex of Sortase A Reveals How Calcium Binding and Substrate Recognition Cooperate in Substrate Activation

G. Otting, Feng Yang, Xiao Wang, 2023, ACS Catalysis.

Numbat: an interactive software tool for fitting Δχ-tensors to molecular coordinates using pseudocontact shifts

G. Otting, T. Huber, C. Schmitz, 2008, Journal of biomolecular NMR.

4,4'-dithiobisdipicolinic acid: a small and convenient lanthanide binding tag for protein NMR spectroscopy.

G. Otting, T. Huber, Xinying Jia, 2011, Chemistry.

3-Mercapto-2,6-pyridinedicarboxylic acid: a small lanthanide-binding tag for protein studies by NMR spectroscopy.

G. Otting, T. Huber, B. Messerle, 2010, Chemistry.

Paramagnetic labelling of proteins and oligonucleotides for NMR

G. Otting, Xuncheng Su, 2010, Journal of biomolecular NMR.

Monitoring the purification by high-performance liquid chromatography of cardiotoxins from Naja mossambica mossambica using phase-sensitive two-dimensional nuclear magnetic resonance.

K. Wüthrich, G. Otting, P. Bougis, 1987, European journal of biochemistry.

Complete protein fingerprints by double-quantum spectroscopy

K. Wüthrich, G. Otting, 1986 .

Interaction of the replication terminator protein of Bacillus subtilis with DNA probed by NMR spectroscopy.

J. Wilce, G. Otting, M. Wilce, 2005, Biochemical and biophysical research communications.

Residual dipolar (1)H-(1)H couplings of methyl groups in weakly aligned proteins.

G. Otting, A. Kaikkonen, 2001, Journal of the American Chemical Society.

New Lanthanide Tag for the Generation of Pseudocontact Shifts in DNA by Site-Specific Ligation to a Phosphorothioate Group.

G. Otting, J. Swarbrick, M. Dennis, 2017, Bioconjugate chemistry.

Sequential NMR assignments of labile protons in DNA using two-dimensional nuclear-Overhauser-enhancement spectroscopy with three jump-and-return pulse sequences.

K. Wüthrich, B. Sproat, G. Otting, 1987, European journal of biochemistry.

Cell‐free synthesis of 15N‐labeled proteins for NMR studies

N. Dixon, G. Otting, K. Ozawa, 2005, IUBMB life.

Contributions from hydration of carboxylate groups to the spectrum of water-polypeptide proton-proton Overhauser effects in aqueous solution

K. Wüthrich, G. Otting, E. Liepinsh, 1993, Journal of biomolecular NMR.

Accurate Electron-Nucleus Distances from Paramagnetic Relaxation Enhancements.

G. Otting, H. Orton, 2018, Journal of the American Chemical Society.