B. Huyghues-Despointes

发表

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 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.

Measurements of disulfide bond stabilities in protein folding intermediates.

B. Huyghues-Despointes, J. W. Nelson, 1990 .

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.

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.

Arabidopsis Vegetative Storage Protein Is an Anti-Insect Acid Phosphatase

B. Huyghues-Despointes, S. Datta, B. Pittendrigh, 2005, Plant Physiology.

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

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

Helical peptides with three pairs of Asp‐Arg and Glu‐Arg residues in different orientations and spacings

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

Stabilities of disulfide bond intermediates in the folding of apamin.

B. Huyghues-Despointes, J. W. Nelson, 1992, Biochemistry.

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.

Measuring the conformational stability of a protein by hydrogen exchange.

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

Measuring the conformational stability of a protein by NMR.

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

Protein conformational stabilities can be determined from hydrogen exchange rates

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

Ion-pair and charged hydrogen-bond interactions between histidine and aspartate in a peptide helix.

R. L. Baldwin, B. Huyghues-Despointes, 1997, Biochemistry.

Measuring the strength of side-chain hydrogen bonds in peptide helices: the Gln.Asp (i, i + 4) interaction.

R. L. Baldwin, T. Klingler, B. Huyghues-Despointes, 1995, 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.

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

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

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.

Single-molecule electrophoresis of beta-hairpin peptides by electrical recordings and Langevin dynamics simulations.

Serdal Kirmizialtin, L. Movileanu, B. Huyghues-Despointes, 2007, The journal of physical chemistry. B.