Richard L. Thurlkill, Ph.D.
Affiliations: | 2005 | Texas A & M University, College Station, TX, United States |
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BiochemistryGoogle:
"Richard Thurlkill"Mean distance: (not calculated yet)
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Sign in to add mentorNick Pace | grad student | 2005 | Texas A & M | |
(Factors determining the pKa values of the ionizable groups in proteins: Their intrinsic pKas and the effects of hydrogen bonding on buried carboxyl groups.) |
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Publications
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Thurlkill RL, Trevino SR, Scholtz JM, et al. (2023) Determining the Conformational Stability of a Protein from Urea and Thermal Unfolding Curves. Current Protocols. 3: e723 |
Pace CN, Fu H, Lee Fryar K, et al. (2014) Contribution of hydrogen bonds to protein stability. Protein Science : a Publication of the Protein Society. 23: 652-61 |
Grimsley GR, Trevino SR, Thurlkill RL, et al. (2013) Determining the conformational stability of a protein from urea and thermal unfolding curves. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit28.4 |
Thurlkill RL, Grimsley GR, Scholtz JM, et al. (2006) Hydrogen bonding markedly reduces the pK of buried carboxyl groups in proteins. Journal of Molecular Biology. 362: 594-604 |
Thurlkill RL, Grimsley GR, Scholtz JM, et al. (2006) pK values of the ionizable groups of proteins. Protein Science : a Publication of the Protein Society. 15: 1214-8 |
Trevino SR, Gokulan K, Newsom S, et al. (2005) Asp79 makes a large, unfavorable contribution to the stability of RNase Sa. Journal of Molecular Biology. 354: 967-78 |
Huyghues-Despointes BM, Thurlkill RL, Daily MD, et al. (2003) pK values of histidine residues in ribonuclease Sa: effect of salt and net charge. Journal of Molecular Biology. 325: 1093-105 |
Laurents DV, Huyghues-Despointes BM, Bruix M, et al. (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: 1077-92 |