C. Nick Pace

C. Nick Pace

Distinguished Professor, Regents Professor, McMullin Professor of Genetics

Department of Molecular and Cellular Medicine
Phone: 979.845.1788

Education and Post-Graduate Training

Dr. Nick Pace received his BS in chemistry from the University of Utah in 1962, and his PhD in biochemistry from Duke University in 1966 working with Dr. Charles Tanford. His postdoctoral work was in the chemistry department at Cornell University working with Dr. Gordon Hammes. He joined the faculty at Texas A&M in 1968. In 1982 he took a sabbatical at the MRC Centre in Cambridge England working with Dr. Tom Creighton and Dr. Alan Barrett. In 1992 he was a visiting professor at Osaka University in the Institute for Protein Research.

Research Interests

The important tasks in living cells are carried out by proteins in which the polypeptide chain is folded into a globular structure that is essential for their biological function. The amino acid sequence of the protein determines the folded structure. Proteins can now be constructed with any desired amino acid sequence. The potential applications of this technology in health and other areas are limited only by our knowledge and imagination. We try to learn how changes in the amino acid sequence effect the structure, function, solubility, and stability of a protein. Our ultimate goal is to be able to predict the folded structure of a protein given just the amino acid sequence.


  • Grimsley, G.R., Scholtz, J.M., and Pace, C.N. (2009) A summary of the measured pK values of the ionizable groups in folded proteins. Protein Sci. 18(1): 247-251.
  • Pace, C.N., Grimsley, G.R., and Scholtz, J.M. (2009) Protein ionizable groups: pK values and their contribution to protein stability and solubility. J Biol Chem. Jan 21. [Epub ahead of print]
  • Trevino, S.R., Scholtz, J.M., and Pace, C.N. (2008) Measuring and increasing protein solubility. J. Pharm. Sci. 97(10): 4155-4166. Review.
  • Alston, R.W., Lasagna, M., Grimsley, G.R., Scholtz, J.M., Reinhart, G.D., and Pace, C.N. (2008) Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa. Biophys. J. 94(6): 2288-2296.
  • Trevino, S.R., Schaefer, S., Scholtz, J.M., and Pace, C.N. (2007) Increasing protein conformational stability by optimizing beta-turn sequence. J. Mol. Biol. 373(1):211-218.
  • Trevino, S., Scholtz, J.M., and Pace, C.N. (2007) Amino Acid Contribution to Protein Solubility: Asp, Glu, and Ser Contribute More Favorably than the other Hydrophillic Amino Acids in Ribonuclease Sa. J. Mol. Biol. 366, 449-460.