Jeffrey K. Myers

Jeffrey Myers received his B.S. in chemistry at The Ohio State University in 1992. He received a Ph.D. in Biochemistry and Biophysics from Texas A&M University in 1996. His thesis work focused on the stability and formation of alpha helical structure in proteins and short peptides.

Dr. Myers continued his research on protein folding and stability as an NIH postdoctoral fellow at Duke University. While at Duke, he experimentally investigated the folding mechanisms of small, mainly helical proteins and worked on theoretical models to describe their folding. Dr. Myers left to join the faculty of Vanderbilt University in 2003 as a Research Assistant Professor. While at Vanderbilt, he investigated the structure and folding of polytopic membrane proteins, and developed an interest in the relationship between the misfolding of proteins and disease.

Dr. Myers has started as a Visiting Professor in the Chemistry Department at the College of Wooster in the fall of 2007.

Selected Publications (out of 24 total):

Myers JK, Mobley CK, Sanders CR. 2007. Folding, misfolding and metal binding of peripheral myelin protein 22 and two mutants related to human neuropathy. Manuscript in preparation.

Mobley CK, Myers JK, Ellis C, Hadzilemovic A, Sanders CR. 2007. Expression, purification, and initial structural characterization of human peripheral myelin protein 22, a tetraspan membrane protein implicated in peripheral neuropathy. Biochemistry, in the press.

Myers JK, Beihoffer L, Sanders CR. 2005. Phenotology of disease-linked proteins. Human Mutation, 25:90-97.

Sanders CR, Myers JK. 2004. Disease-related misassembly of membrane proteins. Annual Review of Biophysics and Biomolecular Structure 33:25-51.

Dimitriadis G, Drysdale A, Myers JK, Arora P, Radford SE, Oas TG, Smith DA. 2004. Microsecond folding dynamics of the F13W/G29A variant of the B-domain of protein A by laser-induced temperature jump. Proc. Natl. Acad. Sci. USA 101:3809-3814.

Myers JK, Oas TG. 2002. Mechanisms of fast protein folding. Annual Review of Biochemistry 71:783-815.

Myers JK, Morris DP, Greenleaf AR, Oas TG. 2001. Phosphorylation of RNApol II CTD fragments results in tight binding to the WW domain of the yeast prolyl isomerase Ess1. Biochemistry 40:8479-8486.

Myers JK, Oas TG. 2001. Pre-organized secondary structure as an important determinant of fast protein folding. Nature Structural Biology 8:552-558.

Myers JK, Oas TG. 1999. Reinterpretation of GCN4-p1 folding kinetics: Partial helix formation precedes dimerization in coiled coil folding. Journal of Molecular Biology 289:205-209.

Myers JK, Pace CN, Scholtz JM. 1997. A direct comparison of helix propensity in proteins and peptides. Proc. Natl. Acad. Sci. USA 94:2833-2837.

Myers JK, Pace CN. 1996. Hydrogen bonding stabilizes globular proteins. Biophysical Journal 71: 2033-2039.

Myers JK, Pace CN, Scholtz JM. 1995. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Science 4:2138-2148.