title: Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa.
abstract: Gaining a better understanding of the denatured state ensemble of proteins is important for understanding protein stability and the mechanism of protein folding. We studied the folding kinetics of ribonuclease Sa (RNase Sa) and a charge-reversal variant (D17R). The refolding kinetics are similar, but the unfolding rate constant is 10-fold greater for the variant. This suggests that charge-charge interactions in the denatured state and the transition state ensembles are more favorable in the variant than in RNase Sa, and shows that charge-charge interactions can influence the kinetics and mechanism of protein folding.
authors.affiliation: Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-1114, USA.
authors.forename: Jared M
authors.initials: JM
authors.lastname: Trefethen
authors.forename: C Nick
authors.initials: CN
authors.lastname: Pace
authors.forename: J Martin
authors.initials: JM
authors.lastname: Scholtz
authors.forename: David N
authors.initials: DN
authors.lastname: Brems
mesh_terms: D004795:Enzyme Stability; D007527:Isoenzymes / Q000737:chemistry* / Q000235:genetics; D007700:Kinetics; D009154:Mutation / Q000235:genetics; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D012260:Ribonucleases / Q000737:chemistry* / Q000235:genetics
chemical_list: D007527:Isoenzymes; D012260:Ribonucleases; C077002:ribonuclease Sa3