Dr. Richard Thurlkill
Assistant Professor of Biochemistry
(325) 942-2181, Ext. 227
E-mail: richard.thurlkill@angelo.edu
Education
Ph.D., Texas A&M University (Biochemistry, 2005)
B.S., Louisiana Tech University (Chemistry, 1986)
Courses taught:
CHEM 1411, CHEM 1412, CHEM 4331 and CHEM 4233
Research Interests
In order to be biologically active most proteins must fold into some three dimensional conformation. This folding sometimes buries ionizable groups, such as carboxyl or imidazole groups, in the interior of the protein away from exposure to bulk water, resulting in large perturbations in the pKa values of those groups.
Our interest is to explore in detail the local effects that induce the perturbations on these groups. To that end we apply traditional protein conformational stability studies along with potentiometric titrations and site-directed mutagenesis to selectively change the local environments around these groups and evaluate the pKa values of those groups in the new environment. Another interest deals with applying mathematical models to evaluate the stability of folded proteins. Our interest here is to study the mathematical models from an experimental point of view in an effort to assist theoreticians in adjusting the models for better agreement with experiment. Here again we apply site-directed mutagenesis and traditional protein conformational stability techniques in our evaluations.
Selected Recent Publications:
Thurlkill, RL, Grimsley, GR, Scholtz, JM, Pace, CN., Hydrogen bonding markedly reduces the pK of buried carboxyl groups in proteins. J Mol Biol, 2006, 362(3): p. 594-604.
Thurlkill, RL, Grimsley, GR, Scholtz, JM, Pace, CN. pK values of the ionizable groups of proteins. Protein Sci, 2006, 15(5): p. 1214-8.
Trevino, SR, Gokulan, K, Newsom, S, Thurlkill, RL, Shaw, KL, Mitkevich, VA, Makarov, AA, Sacchettini, JC, Scholtz, JM, Pace, CN. Asp79 makes a large, unfavorable contribution to the stability of RNase Sa. J Mol Biol, 2005, 354(4): p. 967-78.
Thurlkill, RL, Scholtz, JM, Pace, CN, Cross, DA. The pKa of fentanyl varies with temperature: Implications for acid-base management during extremes of body temperature. J Cardiothorac Vasc Anesth, 2005. 19: p. 759-62.
Huyghues-Despointes, BM, Thurlkill, RL, Daily, MD, Schell, D, Briggs, JM, Antosiewicz, JM, Pace, CN, and Scholtz, JM. pK values of histidine residues in ribonuclease Sa: effect of salt and net charge. J Mol Biol, 2003. 325(5): p. 1093-105.
Laurents, DV, Huyghues-Despointes, BM, Bruix, M, Thurlkill, RL, Schell, D, Newsom, S, Grimsley, GR, Shaw, KL, Trevino, S, Rico, M, Briggs, JM, Antosiewicz, JM, Scholtz, JM, and Pace, CN. Charge-charge interactions are key determinants of the pK values of ionizable groups in ribonuclease Sa (pl=3.5) and a basic variant (pl=10.2). J Mol Biol, 2003. 325(5): p. 1077-92.