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Forces stabilizing proteins

FEBS letters, 2014-06, Vol.588 (14), p.2177-2184

2014

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Toward a Molecular Understanding of Protein Solubility: Increased Negative Surface Charge Correlates with Increased Solubility

Biophysical journal, 2012-04, Vol.102 (8), p.1907-1915

2012

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

The Journal of biological chemistry, 2009-05, Vol.284 (20), p.13285-13289

2009

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

Protein science, 2009-01, Vol.18 (1), p.247-251

2009

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Contribution of hydrogen bonds to protein stability

Protein science, 2014-05, Vol.23 (5), p.652-661

2014

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Contribution of Hydrophobic Interactions to Protein Stability

Journal of molecular biology, 2011-05, Vol.408 (3), p.514-528

2011

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Protein structure, stability and solubility in water and other solvents

Philosophical transactions of the Royal Society of London. Series B. Biological sciences, 2004-08, Vol.359 (1448), p.1225

2004

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Amino Acid Contribution to Protein Solubility: Asp, Glu, and Ser Contribute more Favorably than the other Hydrophilic Amino Acids in RNase Sa

Journal of molecular biology, 2007-02, Vol.366 (2), p.449-460

2007

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pK values of the ionizable groups of proteins

Protein science, 2006-05, Vol.15 (5), p.1214-1218

2006

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Increasing protein stability by improving beta-turns

Proteins, structure, function, and bioinformatics, 2009-11, Vol.77 (3), p.491-498

2009

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Energetics of protein hydrogen bonds

Nature structural & molecular biology, 2009-07, Vol.16 (7), p.681-682

Pace, C Nick

2009

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

Protein science, 2010-05, Vol.19 (5), p.929-943

2010

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Charge–charge interactions influence the denatured state ensemble and contribute to protein stability

Protein science, 2000-07, Vol.9 (7), p.1395-1398

2000

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Peptide Sequence and Conformation Strongly Influence Tryptophan Fluorescence

Biophysical journal, 2008-03, Vol.94 (6), p.2280-2287

2008

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

The Journal of biological chemistry, 2003-08, Vol.278 (34), p.31790-31795

2003

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

Protein science, 2005-07, Vol.14 (7), p.1934-1938

2005

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Tryptophan Fluorescence Reveals the Presence of Long-Range Interactions in the Denatured State of Ribonuclease Sa

Biophysical journal, 2008-03, Vol.94 (6), p.2288-2296

2008

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Measuring and Increasing Protein Solubility

Journal of pharmaceutical sciences, 2008-10, Vol.97 (10), p.4155-4166

2008

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Increasing Protein Conformational Stability by Optimizing β-Turn Sequence

Journal of molecular biology, 2007-10, Vol.373 (1), p.211-218

2007

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A Helix Propensity Scale Based on Experimental Studies of Peptides and Proteins

Biophysical journal, 1998-07, Vol.75 (1), p.422-427

1998

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Changing the net charge from negative to positive makes ribonuclease Sa cytotoxic

Protein science, 2002-10, Vol.11 (10), p.2522-2525

2002

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Contribution of Single Tryptophan Residues to the Fluorescence and Stability of Ribonuclease Sa

Biophysical journal, 2004-12, Vol.87 (6), p.4036-4047

2004

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A Direct Comparison of Helix Propensity in Proteins and Peptides

Proceedings of the National Academy of Sciences - PNAS, 1997-04, Vol.94 (7), p.2833-2837

1997

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Polar Group Burial Contributes More to Protein Stability than Nonpolar Group Burial

Biochemistry (Easton), 2001-01, Vol.40 (2), p.310-313

Pace, C. Nick

2001

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Linear extrapolation method of analyzing solvent denaturation curves

Proteins, structure, function, and bioinformatics, 2000, Vol.41 (S4), p.1-7

2000

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Forces stabilizing proteins

Toward a Molecular Understanding of Protein Solubility: Increased Negative Surface Charge Correlates with Increased Solubility

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

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

Contribution of hydrogen bonds to protein stability

Contribution of Hydrophobic Interactions to Protein Stability

Protein structure, stability and solubility in water and other solvents

Amino Acid Contribution to Protein Solubility: Asp, Glu, and Ser Contribute more Favorably than the other Hydrophilic Amino Acids in RNase Sa

pK values of the ionizable groups of proteins

Increasing protein stability by improving beta-turns

Energetics of protein hydrogen bonds

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

Charge–charge interactions influence the denatured state ensemble and contribute to protein stability

Peptide Sequence and Conformation Strongly Influence Tryptophan Fluorescence

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

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

Tryptophan Fluorescence Reveals the Presence of Long-Range Interactions in the Denatured State of Ribonuclease Sa

Measuring and Increasing Protein Solubility

Increasing Protein Conformational Stability by Optimizing β-Turn Sequence

A Helix Propensity Scale Based on Experimental Studies of Peptides and Proteins

Changing the net charge from negative to positive makes ribonuclease Sa cytotoxic

Contribution of Single Tryptophan Residues to the Fluorescence and Stability of Ribonuclease Sa

A Direct Comparison of Helix Propensity in Proteins and Peptides

Polar Group Burial Contributes More to Protein Stability than Nonpolar Group Burial

Linear extrapolation method of analyzing solvent denaturation curves

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