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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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How to measure and predict the molar absorption coefficient of a protein

Protein science, 1995-11, Vol.4 (11), p.2411-2423

1995

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Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding

Protein science, 1995-10, Vol.4 (10), p.2138-2148

1995

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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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Conformational stability of globular proteins

Trends in Biochemical Sciences, 1990, Vol.15 (1), p.14-17

Pace, C.Nick

1990

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Measuring and increasing protein stability

Trends in biotechnology (Regular ed.), 1990-04, Vol.8 (4), p.93-98

Pace, C. Nick

1990

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Increasing protein stability by altering long-range coulombic interactions

Protein science, 1999-09, Vol.8 (9), p.1843-1849

1999

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Contribution of the hydrophobic effect to globular protein stability

Journal of molecular biology, 1992-07, Vol.226 (1), p.29-35

Pace, C.Nick

1992

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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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Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds

The Journal of biological chemistry, 1988-08, Vol.263 (24), p.11820-11825

1988

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[24] Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding

Methods in Enzymology, 1995, Vol.259, p.538-554

Pace, C.N.

1995

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Contribution of hydrogen bonding to the conformational stability of ribonuclease T1

Biochemistry (Easton), 1992-01, Vol.31 (3), p.725-732

1992

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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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Heat capacity change for ribonuclease A folding

Protein science, 1999-07, Vol.8 (7), p.1500-1504

1999

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Protein conformational stabilities can be determined from hydrogen exchange rates

Nature structural biology, 1999-10, Vol.6 (10), p.910-912

1999

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Forces contributing to the conformational stability of proteins

The FASEB journal, 1996-01, Vol.10 (1), p.75-83

1996

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Cytotoxicity mechanism of the RNase Sa cationic mutants involves inhibition of potassium current through Ca2+-activated channels

Molekuliarnaia biologiia, 2015-11, Vol.49 (6), p.1041

2015

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The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

Protein science, 2001-06, Vol.10 (6), p.1206-1215

2001

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[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves

Methods in Enzymology, 1986, Vol.131, p.266-280

Pace, C.N.

1986

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Hydrogen bonding stabilizes globular proteins

Biophysical journal, 1996-10, Vol.71 (4), p.2033-2039

1996

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Urea denaturation of barnase: pH dependence and characterization of the unfolded state

Biochemistry (Easton), 1992-03, Vol.31 (10), p.2728-2734

1992

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Single surface stabilizer

Nature structural & molecular biology, 2000-05, Vol.7 (5), p.345-346

Pace, C. Nick

2000

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Tyrosine hydrogen bonds make a large contribution to protein stability

Journal of molecular biology, 2001-09, Vol.312 (2), p.393-404

2001

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Conformational stability and mechanism of folding of ribonuclease T1

The Journal of biological chemistry, 1989-07, Vol.264 (20), p.11614-11620

1989

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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)

Journal of molecular biology, 2003-01, Vol.325 (5), p.1077-1092

2003

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

How to measure and predict the molar absorption coefficient of a protein

Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding

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

Conformational stability of globular proteins

Measuring and increasing protein stability

Increasing protein stability by altering long-range coulombic interactions

Contribution of the hydrophobic effect to globular protein stability

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

Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds

[24] Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding

Contribution of hydrogen bonding to the conformational stability of ribonuclease T1

Linear extrapolation method of analyzing solvent denaturation curves

Heat capacity change for ribonuclease A folding

Protein conformational stabilities can be determined from hydrogen exchange rates

Forces contributing to the conformational stability of proteins

Cytotoxicity mechanism of the RNase Sa cationic mutants involves inhibition of potassium current through Ca2+-activated channels

The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves

Hydrogen bonding stabilizes globular proteins

Urea denaturation of barnase: pH dependence and characterization of the unfolded state

Single surface stabilizer

Tyrosine hydrogen bonds make a large contribution to protein stability

Conformational stability and mechanism of folding of ribonuclease T1

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)

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