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FOR THE RECORD

Charge–charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa

¹ Department of Biochemistry and Biophysics, and ² Department of Medical Biochemistry and Genetics, Texas A&M University, College Station, Texas 77843, USA
³ Department of Pharmaceutics, Amgen, Inc., Thousand Oaks, California 91320, USA

(RECEIVED February 8, 2005; FINAL REVISION April 13, 2005; ACCEPTED April 17, 2005)

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.

Keywords: protein folding; protein stability; folding kinetics; denatured state; charge–charge interactions

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051401905.

Reprint requests to: C.N. Pace, 440 Reynolds Medical Building, Texas A&M University, College Station, TX 77843-1114, USA; e-mail: nickpace{at}tamu.edu; fax: (979) 847-9481; or J.M. Scholtz, 440 Reynolds Medical Building, Texas A&M University, College Station, TX 77843-1114, USA; e-mail: jm-scholtz{at}tamu.edu; fax: (979) 847-9481.

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