Scholtz, J. Martin individual record
Executive Associate Vice President for Research
overview

Currently, research in the Scholtz laboratory is in several areas related to protein folding and misfolding. In these studies we make extensive use of a battery of biophysical techniques including NMR, differential scanning calorimetry, fluorescence and visible spectroscopy and circular dichroism spectroscopy. In addition, we routinely employ molecular biology and protein chemistry techniques to produce and purify recombinant proteins and use automated peptide synthesis for the production of synthetic peptides.

selected publications
Academic Articles106
Chapters3
  • Grimsley, G. R., Trevino, S. R., Thurlkill, R. L., & Scholtz, J. M. (2013). Determining the conformational stability of a protein from urea and thermal unfolding curves.. Current Protocols in Protein Science. (pp. Unit28.4-28.4.14). Wiley.
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  • Scholtz, J. M., Grimsley, G. R., & Pace, C. N. (2009). SOLVENT DENATURATION OF PROTEINS AND INTERPRETATIONS OF THE M VALUE. GUIDE TO TECHNIQUES IN MOUSE DEVELOPMENT, PT A: MICE, EMBRYOS, AND CELLS, 2ND EDITION. METHODS IN ENZYMOLOGY, VOL 466: BIOTHERMODYNAMICS, PT B. (pp. 549-565). Elsevier.
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  • Pace, C. N., Grimsley, G. R., & Scholtz, J. M. (2008). Denaturation of Proteins by Urea and Guanidine Hydrochloride. Protein Folding Handbook. (pp. 45-69). Wiley-VCH Verlag GmbH.
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Conference Papers4
chaired theses and dissertations
Email
scholtz@tamu.edu
First Name
J. Martin
Last Name
Scholtz
mailing address
Texas A&M University; Vice Pres For Research; 1112 TAMU
College Station, TX 77843-1112
USA