Article
Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa.
Protein science : a publication of the Protein Society - 1 Jul 2005
Trefethen Jared M, Pace C Nick, Scholtz J Martin, Brems David N
Abstract excerpt
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...
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