J. Martin Scholtz
professor
Biochemistry and Biophysics
Texas A and M University
United States of America
Biography
Ph.D. University of California, Berkeley (1989) Postdoc. Stanford University (1989-93) Joined Texas A&M in 1993
Research Interest
We are interested in the problem of protein folding – a description of the mechanism by which a protein adopts a given three dimensional structure using only the information encoded in the primary sequence of amino acids. We are currently testing the idea that protein folding and stability can be described in a hierarchical fashion: building stability and structure from the primary sequence through secondary structure to the tertiary structure of proteins. Toward this end, our efforts have concentrated on the role helix stability plays in governing protein folding and stability in several model proteins.
Publications
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Grimsley, GR, Trevino, SR, Thurlkill, RL, Scholtz, JM. Determining the conformational stability of a protein from urea and thermal unfolding curves. Curr Protoc Protein Sci. 2013;Chapter 28 :Unit28.4. doi: 10.1002/0471140864.ps2804s71. PubMed PMID:23377851. .
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Pace, CN, Fu, H, Lee Fryar, K, Landua, J, Trevino, SR, Schell, D et al.. Contribution of hydrogen bonds to protein stability. Protein Sci. 2014;23 (5):652-61. doi: 10.1002/pro.2449. PubMed PMID:24591301. PubMed Central PMC4005716.
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Nick Pace, C, Scholtz, JM, Grimsley, GR. Forces stabilizing proteins. FEBS Lett. 2014;588 (14):2177-84. doi: 10.1016/j.febslet.2014.05.006. PubMed PMID:24846139. PubMed Central PMC4116631.
