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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).
Laurents DV, Huyghues-Despointes BM, Bruix M, Thurlkill RL, Schell D, Newsom S, Grimsley GR, Shaw KL, Treviño S, Rico M, Briggs JM, Antosiewicz JM, Scholtz JM, Pace CN. Laurents DV, et al. Among authors: pace cn. J Mol Biol. 2003 Jan 31;325(5):1077-92. doi: 10.1016/s0022-2836(02)01273-1. J Mol Biol. 2003. PMID: 12527309
Asp79 makes a large, unfavorable contribution to the stability of RNase Sa.
Trevino SR, Gokulan K, Newsom S, Thurlkill RL, Shaw KL, Mitkevich VA, Makarov AA, Sacchettini JC, Scholtz JM, Pace CN. Trevino SR, et al. Among authors: pace cn. J Mol Biol. 2005 Dec 9;354(4):967-78. doi: 10.1016/j.jmb.2005.09.091. Epub 2005 Oct 21. J Mol Biol. 2005. PMID: 16288913
Contribution of hydrophobic interactions to protein stability.
Pace CN, Fu H, Fryar KL, Landua J, Trevino SR, Shirley BA, Hendricks MM, Iimura S, Gajiwala K, Scholtz JM, Grimsley GR. Pace CN, et al. J Mol Biol. 2011 May 6;408(3):514-28. doi: 10.1016/j.jmb.2011.02.053. Epub 2011 Mar 4. J Mol Biol. 2011. PMID: 21377472 Free PMC article.
108 results