G. Grimsley

发表

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

Kevin L. Shaw, C. Pace, A. Makarov, 2001, Protein science : a publication of the Protein Society.

Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3.

K S Wilson, Kevin L. Shaw, Z Dauter, 1998, Journal of molecular biology.

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.

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.

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

C. Pace, G. Grimsley, L. Fee, 1995, Protein science : a publication of the Protein Society.

Contribution of hydrophobic interactions to protein stability.

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

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.

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.

Spectrophotometric Determination of Protein Concentration

C. Pace, G. Grimsley, 2003, Current protocols in protein science.

Purification of ribonuclease T1.

C. Pace, G. Grimsley, B. Barnett, 1987, Analytical biochemistry.

Contribution of hydrogen bonds to protein stability

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

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.

Denaturation of Proteins by Urea and Guanidine Hydrochloride

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

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.

Solvent denaturation of proteins and interpretations of the m value.

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

pK values of the ionizable groups of proteins

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

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.

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.

Purification of ribonucleases Sa, Sa2, and Sa3 after expression in Escherichia coli.

C. Pace, R. Hartley, G. Grimsley, 1997, Protein expression and purification.

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.

Heat capacity change for ribonuclease A folding

S. T. Thomas, C. Pace, G. Makhatadze, 1999, Protein science : a publication of the Protein Society.

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

C. Pace, J. Thomson, G. Grimsley, 1988, The Journal of biological chemistry.

Measuring the conformational stability of a protein by NMR.

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

Peptide sequence and conformation strongly influence tryptophan fluorescence.

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

Conformational stability and mechanism of folding of ribonuclease T1.

C. Pace, B. Shirley, J. Thomson, 1989, The Journal of biological chemistry.

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.

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

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