J. M. Scholtz

发表

Urea unfolding of peptide helices as a model for interpreting protein unfolding.

R. L. Baldwin, J. M. Scholtz, D. Barrick, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Parameters of helix–coil transition theory for alanine‐based peptides of varying chain lengths in water

R. L. Baldwin, J. M. Scholtz, E. York, 1991, Biopolymers.

Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate.

C. Pace, J. M. Scholtz, J. Grimsley, 1997, Biochemistry.

Protein structure, stability and solubility in water and other solvents.

C. Pace, J. M. Scholtz, E. Prabhakaran, 2004, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

Increasing protein stability by altering long‐range coulombic interactions

Kevin L. Shaw, C. Pace, J. M. Scholtz, 1999, Protein science : a publication of the Protein Society.

Charge–charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa

C. Pace, J. M. Scholtz, D. Brems, 2005, Protein science : a publication of the Protein Society.

Increasing protein stability by improving beta‐turns

C. Pace, J. M. Scholtz, G. Grimsley, 2009, Proteins.

Forces stabilizing proteins

C. Pace, J. M. Scholtz, C. Nick Pace, 2014, FEBS letters.

Contribution of hydrophobic interactions to protein stability.

C. Pace, B. Shirley, K. Gajiwala, 2011, Journal of molecular biology.

Tyrosine hydrogen bonds make a large contribution to protein stability.

Kevin L. Shaw, C. Pace, J. M. Scholtz, 2001, Journal of molecular biology.

A helix propensity scale based on experimental studies of peptides and proteins.

C. Pace, J. M. Scholtz, J. Scholtz, 1998, Biophysical journal.

A summary of the measured pK values of the ionizable groups in folded proteins

C. Pace, J. M. Scholtz, G. Grimsley, 2008, Protein science : a publication of the Protein Society.

A neutral, water-soluble, .alpha.-helical peptide: the effect of ionic strength on the helix-coil equilibrium

R. L. Baldwin, J. M. Scholtz, E. York, 1991 .

Charge-charge interactions are key determinants of the pK values of ionizable groups in ribonuclease Sa (pI=3.5) and a basic variant (pI=10.2).

David Schell, Kevin L. Shaw, D. Laurents, 2003, Journal of molecular biology.

Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins

Kazufumi Takano, J. M. Scholtz, K. Takano, 2010, Protein science : a publication of the Protein Society.

Hydrogen bonding increases packing density in the protein interior

David Schell, Jerry Tsai, J. Tsai, 2005, Proteins.

Hydrogen bonding of beta-turn structure is stabilized in D(2)O.

J. M. Scholtz, A. Chilkoti, P. Cremer, 2009, Journal of the American Chemical Society.

2,3-Methanoamino acid analogs of Arg stabilize secondary structures of a 13 amino acid peptide in aqueous solution

J. M. Scholtz, K. Burgess, D. Lim, 1998 .

Rat liver 4-hydroxy-2-ketoglutarate aldolase: purification and kinetic characterization.

S. Schuster, J. M. Scholtz, M. Anderson, 1985, Archives of biochemistry and biophysics.

General Principles and Pharmacology of Antineoplastic Agents

J. M. Scholtz, J. Scholtz, 1991 .

Differential Binding Energy: A Detailed Evaluation of the Influence of Hydrogen-Bonding and Hydrophobic Groups on the Inhibition of Thermolysin by Phosphorus-Containing Inhibitors.

J. M. Scholtz, P. Bartlett, M. Ballinger, 1991 .

CHARACTERIZATION OF Mycobacterium tuberculosis CmtR,

J. M. Scholtz, P. Lindahl, D. O. Peterson, 2005 .

Substrates of hydroxyketoglutarate aldolase

S. Schuster, J. M. Scholtz, 1984 .

Calorimetric determination of the enthalpy change for the a-helix to coil transition of an alanine peptide in water ( L-alanine helix / peptide hydrogen bond / helix-coil enthalpy )

R. L. Baldwin, S. Marqusee, J. M. Scholtz, 2022 .

Perchlorate-induced denaturation of ribonuclease A: investigation of possible folding intermediates.

R. L. Baldwin, J. M. Scholtz, J. Scholtz, 1993, Biochemistry.

Synthesis and evaluation of inhibitors for Escherichia coli carbamyl phosphate synthetase

J. M. Scholtz, P. Bartlett, 1989 .

Helix propensities are identical in proteins and peptides.

C. Pace, J. M. Scholtz, J. Myers, 1997, Biochemistry.

Hydrogen-exchange stabilities of RNase T1 and variants with buried and solvent-exposed Ala --> Gly mutations in the helix.

C. Pace, J. M. Scholtz, J. Steyaert, 1999, Biochemistry.

Toward a molecular understanding of protein solubility: increased negative surface charge correlates with increased solubility.

C. Pace, J. M. Scholtz, C Nick Pace, 2012, Biophysical journal.

Differential binding energy: a detailed evaluation of the influence of hydrogen-bonding and hydrophobic groups on the inhibition of thermolysin by phosphorus-containing inhibitors

Paul A. Bartlett, Bradley P. Morgan, J. M. Scholtz, 1991 .

Contribution of hydrogen bonds to protein stability

C. Pace, B. Shirley, K. Gajiwala, 2014, Protein science : a publication of the Protein Society.

pK values of histidine residues in ribonuclease Sa: effect of salt and net charge.

Michael D. Daily, J. Briggs, J. Antosiewicz, 2003, Journal of molecular biology.

The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide.

R. L. Baldwin, J. M. Scholtz, H. Qian, 1993, Biochemistry.

Carbodiimide EDC induces cross-links that stabilize RNase A C-dimer against dissociation: EDC adducts can affect protein net charge, conformation, and activity.

D. Laurents, J. M. Scholtz, M. Vilanova, 2009, Bioconjugate chemistry.

Distinct Secondary Structures of the Leucine-rich Repeat Proteoglycans Decorin and Biglycan

C. Pace, J. M. Scholtz, P. Krishnan, 1999, The Journal of Biological Chemistry.

The role of protein stability, solubility, and net charge in amyloid fibril formation

J. M. Scholtz, J Martin Scholtz, Jason P Schmittschmitt, 2003, Protein science : a publication of the Protein Society.

Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa.

C. Pace, J. M. Scholtz, C Nick Pace, 2007, Journal of molecular biology.

Protein Ionizable Groups: pK Values and Their Contribution to Protein Stability and Solubility*

C. Pace, J. M. Scholtz, G. Grimsley, 2009, Journal of Biological Chemistry.

pKa of fentanyl varies with temperature: implications for acid-base management during extremes of body temperature.

C. Pace, J. M. Scholtz, Richard L Thurlkill, 2005, Journal of cardiothoracic and vascular anesthesia.

Factors that influence helical preferences for singly charged gas-phase peptide ions: the effects of multiple potential charge-carrying sites.

C. Pace, J. M. Scholtz, J. McLean, 2010, The journal of physical chemistry. B.

Interactions of peptides with a protein pore.

J. M. Scholtz, H. Bayley, L. Movileanu, 2005, Biophysical journal.

RNase-induced apoptosis: fate of calcium-activated potassium channels.

C. Pace, A. Makarov, J. M. Scholtz, 2008, Biochimie.

Osteopontin is a ligand for the alpha4beta1 integrin.

J. M. Scholtz, G. Davis, K. Bayless, 1998, Journal of cell science.

Lessons in stability from thermophilic proteins

J. M. Scholtz, Abbas Razvi, J Martin Scholtz, 2006, Protein science : a publication of the Protein Society.

Denaturation of Proteins by Urea and Guanidine Hydrochloride

C. Pace, J. M. Scholtz, G. Grimsley, 2008 .

Energetic Implications for Protein Phosphorylation

J. M. Scholtz, M. E. Huffine, J. Scholtz, 1996, The Journal of Biological Chemistry.

Increasing protein stability: Importance of ΔCp and the denatured state

C. Pace, J. M. Scholtz, G. Grimsley, 2010, Protein science : a publication of the Protein Society.

Guanidine hydrochloride unfolding of peptide helices: separation of denaturant and salt effects.

J. M. Scholtz, J. Smith, 1996, Biochemistry.

Solvent denaturation of proteins and interpretations of the m value.

C. Pace, J. M. Scholtz, G. Grimsley, 2009, Methods in enzymology.

Osmolyte effects on helix formation in peptides and the stability of coiled‐coils

J. M. Scholtz, S. Celinski, J. Scholtz, 2002, Protein science : a publication of the Protein Society.

Increasing protein conformational stability by optimizing β-turn sequence

J. Martin Scholtz, C. Pace, J. M. Scholtz, 2007 .

Purification and Biochemical Characterization of the Lambda Holin

J. M. Scholtz, D. Struck, R. Young, 1998, Journal of bacteriology.

pK values of the ionizable groups of proteins

C. Pace, J. M. Scholtz, G. Grimsley, 2006, Protein science : a publication of the Protein Society.

The mechanism of alpha-helix formation by peptides.

R. L. Baldwin, J. M. Scholtz, R L Baldwin, 1992, Annual review of biophysics and biomolecular structure.

Osteopontin is a ligand for the α 4 β 1 integrin

J. M. Scholtz, G. Davis, K. Bayless, 1998 .

Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa.

C. Pace, J. M. Scholtz, G. Reinhart, 2008, Biophysical journal.

NMR study and molecular dynamics simulations of optimized β‐hairpin fragments of protein G

J. Tsai, J. M. Scholtz, B. Huyghues-Despointes, 2007, Proteins.

4 – α-Helix Formation by Peptides in Water

R. L. Baldwin, J. M. Scholtz, J. Scholtz, 1995 .

Effect of a single aspartate on helix stability at different positions in a neutral alanine‐based peptide

R. L. Baldwin, J. M. Scholtz, B. Huyghues-Despointes, 1993, Protein science : a publication of the Protein Society.

An engineered leucine zipper a position mutant with an unusual three‐state unfolding pathway

James C. Hu, J. M. Scholtz, J M Scholtz, 2001, Protein science : a publication of the Protein Society.

Asp79 makes a large, unfavorable contribution to the stability of RNase Sa.

Kevin L. Shaw, C. Pace, A. Makarov, 2005, Journal of molecular biology.

The Contribution of Polar Group Burial to Protein Stability Is Strongly Context-dependent*

C. Pace, J. M. Scholtz, J. Sacchettini, 2003, Journal of Biological Chemistry.

Charge-charge interactions are the primary determinants of the pK values of the ionizable groups in Ribonuclease T1.

J. Briggs, C. Pace, J. M. Scholtz, 2002, Biophysical chemistry.

Phosphorylation of serine‐46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure

J. M. Scholtz, M. Saier, R. Klevit, 1995, Protein science : a publication of the Protein Society.

A direct comparison of helix propensity in proteins and peptides.

C. Pace, J. M. Scholtz, J. Myers, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Measuring the conformational stability of a protein by hydrogen exchange.

S W Englander, C. Pace, J. M. Scholtz, 2001, Methods in molecular biology.

Determining the Conformational Stability of a Protein from Urea and Thermal Unfolding Curves

J. M. Scholtz, G. Grimsley, J Martin Scholtz, 2013, Current protocols in protein science.

Measuring the conformational stability of a protein by NMR.

C. Pace, J. M. Scholtz, G. Grimsley, 2006, CSH protocols.

Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation.

R. L. Baldwin, C. Rohl, J. M. Scholtz, 1992, Biochemistry.

Protein conformational stabilities can be determined from hydrogen exchange rates

C. Pace, J. M. Scholtz, B. Huyghues-Despointes, 1999, Nature Structural Biology.

Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa.

C. Pace, J. M. Scholtz, G. Reinhart, 2004, Biophysical journal.

A convenient differential protection strategy for functional group manipulation of aspartic and glutamic acids

J. M. Scholtz, P. Bartlett, 1989 .

Peptide sequence and conformation strongly influence tryptophan fluorescence.

C. Pace, J. M. Scholtz, G. Reinhart, 2008, Biophysical journal.

Measuring and increasing protein solubility.

C. Pace, J. M. Scholtz, Saul R. Trevino, 2008, Journal of pharmaceutical sciences.

Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water.

R. L. Baldwin, S. Marqusee, J. M. Scholtz, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Increasing protein conformational stability by optimizing beta-turn sequence.

C. Pace, J. M. Scholtz, C Nick Pace, 2007, Journal of molecular biology.

Terminal ion pairs stabilize the second β‐hairpin of the B1 domain of protein G

J. Tsai, J. M. Scholtz, B. Huyghues-Despointes, 2006 .

Conformational stability of the Escherichia coli HPr protein: test of the linear extrapolation method and a thermodynamic characterization of cold denaturation.

J. M. Scholtz, E. Nicholson, J. Scholtz, 1996, Biochemistry.

Preparation of urea and guanidinium chloride stock solutions for measuring denaturant-induced unfolding curves.

C. Pace, J. M. Scholtz, G. Grimsley, 2006, CSH protocols.

Hydrogen bonding markedly reduces the pK of buried carboxyl groups in proteins.

C. Pace, J. M. Scholtz, G. Grimsley, 2006, Journal of molecular biology.

Influence of N-cap mutations on the structure and stability of Escherichia coli HPr.

J. M. Scholtz, R. Klevit, E. Waygood, 1996, Biochemistry.

The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil.

H. Zhu, J. M. Scholtz, S. Celinski, 2000, Journal of molecular biology.

Regulation of rat liver 4-hydroxy-2-ketoglutarate aldolase.

S. Schuster, J. M. Scholtz, 1986, Biochimica et biophysica acta.

Hydrogen Bonding of-Turn Structure Is Stabilized in D 2 O

J. M. Scholtz, A. Chilkoti, P. Cremer, 2009 .