What is your educational background?
- Ph.D., Texas A&M University
- B.S., Grove City College
- Beginning Biochemistry (CHEM 141)
- Biochemistry I (CHEM 351)
- Biochemistry II (CHEM 352)
- Biochemistry: Data and Analysis (CHEM 451)
- Biochemistry Seminar (CHEM 487)
Proteins are synthesized by ribosomes as a linear sequence of amino acids. The sequence of amino acids in a protein is reflective of the gene sequence that codes for the protein. Beyond the genetic information, the primary structure holds all the information necessary for a protein to fold into an intricate, three-dimensional structure. This three-dimensional structure is the active, functional protein structure. Unlike the genetic code, the "rules" for protein folding are not fully understood.
I am interested in determining the magnitude of the molecular forces that favor the folded protein over the unfolded protein. I am also interested in using an understanding of these forces to increase the folding energy of medically or industrially important proteins. I am also interested in developing and using computational algorithms for protein design.
- C. Nick Pace, Gerald R. Grimsley, J. Martin Scholtz and Kevin L. Shaw. 2014. Protein Stability. In: eLS. John Wiley & Sons Ltd, Chichester.
- Kevin L. Shaw, J. Martin Scholtz, C. Nick Pace, and Gerald R. Grimsley. 2009. Determining the conformational stability of a protein using urea denaturation curves. Methods in Molecular Biology. 490: 41-55.
- Saul R. Trevino, Kuppan Gokulan, Stephanie Newsom, Richard L. Thurlkill, Kevin L. Shaw, Vladimir A. Mitkevich, Alexander A. Makarov, James C. Sacchettini, J. Martin Scholtz, and C. Nick Pace. 2005. Asp79 makes a large, unfavorable contribution to the stability of RNase Sa. Journal of Molecular Biology. 354: 967-978.
- Gennady I. Yakovlev, Vladimir A. Mitkevich, Kevin L. Shaw, Saul Trevino, Stephanie Newsom, C. Nick Pace, and Alexander A. Makarov. 2003. Contribution of active site residues to the activity and thermal stability of ribonuclease Sa. Protein Science. 12: 2367-2373.
- Douglas V. Laurents, Beatrice M. P. Huyghues-Despointes, Marta Bruix, Richard L. Thurlkill, David Schell, Stephanie Newsom, Gerald R. Grimsley, Kevin L. Shaw, Saul Trevino, Manuel Rico, James M. Briggs, Jan M. Antosiewicz, J. Martin Scholtz and C. Nick Pace. 2003. Charge-charge interactions are key determinants of the pK values of ionizable groups in ribonuclease Sa (pI=3.5) and a basic variant (pI=10.2). Journal of Molecular Biology. 325: 1077-1092.
- Olga N. Ilinskaya, Florian Dreyer, Vladimir A. Mitkevich, Kevin L. Shaw, C. Nick Pace, and Alexander A. Makarov. 2002. Changing the net charge from negative to positive makes ribonuclease Sa cytotoxic. Protein Science. 11: 2522-2525.
- C. Nick Pace, Geoffrey Horn, Eric J. Hebert, John Bechert, Kevin Shaw, Lubica Urbanikova, J. Martin Scholtz, and Jozef Sevcik. 2001. Tyrosine hydrogen bonds make a large contribution to protein stability. Journal of Molecular Biology. 312: 393-404.
- Kevin L. Shaw, Gerald R. Grimsley, Gennady Yakovlev, Alexander Makarov, and C. Nick Pace. 2001. The effect of net charge on the solubility, activity, and stability of ribonuclease Sa. Protein Science. 10: 1206-1215.
- C. Nick Pace and Kevin L. Shaw. 2000. Linear extrapolation method of analyzing solvent denaturation curves. Proteins: Structure, Function and Genetics. Suppl 4: 1-7.
- C. Nick Pace, Roy W. Alston and Kevin L. Shaw. 2000. Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. Protein Science. 9: 1395-1398.
- Gerald R. Grimsley, Kevin L. Shaw, Lanette R. Fee, Roy W. Alston, Beatrice M. P. Huyghues-Despointes, Richard L. Thurlkill, J. Martin Scholtz and C. Nick Pace. 1999. Increasing protein stability by altering long-range coulombic interactions. Protein Science. 8: 1843-1849.
- C. Nick Pace, Eric J. Hebert, Kevin L. Shaw, David Schell, Valentin Both, Daniela Krajcikova, Jozef Sevcik, Keith S. Wilson, Zbigniew Dauter, Robert W. Hartley and Gerald R. Grimsley. 1998. Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3. Journal of Molecular Biology. 279: 271-286.
What is the most important piece of advice you give students to help them succeed?
I always encourage students to tackle new problems, not to be afraid to continue learning throughout life, and to be open to variety of possibilities. There will be change, of many more varieties than your area of interest, during your lifetime – be prepared to embrace that change. You will learn throughout your life – the exams will move from three or four a semester to every day. Accept it. Embrace it.