J. Myers

发表

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

C. Pace, J. Myers, C. Nick Pace, 1995, Protein science : a publication of the Protein Society.

Protein folding dynamics: quantitative comparison between theory and experiment.

T. Oas, J. Myers, R. E. Burton, 1998, Biochemistry.

Fast and faster: a designed variant of the B-domain of protein A folds in 3 microsec.

T. Oas, J. Myers, P. Arora, 2004, Protein science : a publication of the Protein Society.

Mechanism of fast protein folding.

T. Oas, J. Myers, 2002, Annual review of biochemistry.

Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1.

T. Oas, A. Greenleaf, J. Myers, 2001, Biochemistry.

Preorganized secondary structure as an important determinant of fast protein folding

Terrence G. Oas, T. Oas, J. Myers, 2001, Nature Structural Biology.

The peripheral neuropathy-linked Trembler and Trembler-J mutant forms of peripheral myelin protein 22 are folding-destabilized.

C. Sanders, J. Myers, Charles K. Mobley, 2008, Biochemistry.

Osmolyte effects on the self-association of concanavalin A: testing theoretical models.

Thomas R. Silvers, J. Myers, 2013, Biochemistry.

Thermodynamics of Concanavalin A Self-Association in the Presence of Osmolytes

J. Myers, T. Pfister, S. Cooper, 2018 .

Phenotology of disease‐linked proteins

C. Sanders, J. Myers, Lauren A. Beihoffer, 2005, Human mutation.

Disease-related misassembly of membrane proteins.

Charles R Sanders, C. Sanders, J. Myers, 2004, Annual review of biophysics and biomolecular structure.

Helix propensities are identical in proteins and peptides.

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

Probing the folding and unfolding dynamics of secondary and tertiary structures in a three-helix bundle protein.

T. Oas, R. Dyer, J. Myers, 2004, Biochemistry.

Hydrogen bonding stabilizes globular proteins.

C. Pace, J. Myers, C N Pace, 1996, Biophysical journal.

Spectroscopic Characterization of Amyloid Fibril Formation by Lysozyme

J. Myers, 2014 .

Protein Fibrillation under Crowded Conditions

J. Myers, Annelise H. Gorensek-Benitez, Bryan Kirk, 2022, Biomolecules.

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.

Protein-RNA interactions: exploring binding patterns with a three-dimensional superposition analysis of high resolution structures

N. Morozova, J. Allers, J. Myers, 2006, Bioinform..

Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump.

Sheena E Radford, S. Radford, G. Dimitriadis, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Contribution of a buried hydrogen bond to lambda repressor folding kinetics.

T. Oas, J. Myers, 1999, Biochemistry.

Fast and faster: A designed variant of the B‐domain of protein A folds in 3 μsec

T. Oas, J. Myers, P. Arora, 2004 .

Reinterpretation of GCN4-p1 folding kinetics: partial helix formation precedes dimerization in coiled coil folding.

T. Oas, J. Myers, 1999, Journal of molecular biology.

Trifluoroethanol effects on helix propensity and electrostatic interactions in the helical peptide from ribonuclease T1

J. Myers, C. Nick Pace, J. Martin Scholtz, 1998, Protein science : a publication of the Protein Society.

The peripheral neuropathy-linked Trembler and Trembler-J mutant forms of peripheral myelin protein 22 are folding-destabilized.

C. Sanders, J. Myers, Charles K. Mobley, 2008, Biochemistry.