Journal article
Charge–charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa
Protein science, Vol.14(7), pp.1934-1938
07/01/2005
DOI: 10.1110/ps.051401905
PMCID: PMC2253365
PMID: 15937282
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.
Details
- Title: Subtitle
- Charge–charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa
- Creators
- Jared M. Trefethen - Texas A&M UniversityC. Nick Pace - Texas A&M UniversityJ. Martin Scholtz - Texas A&M UniversityDavid N. Brems - Amgen (United States)
- Resource Type
- Journal article
- Publication Details
- Protein science, Vol.14(7), pp.1934-1938
- DOI
- 10.1110/ps.051401905
- PMID
- 15937282
- PMCID
- PMC2253365
- NLM abbreviation
- Protein Sci
- ISSN
- 0961-8368
- eISSN
- 1469-896X
- Publisher
- Cold Spring Harbor Laboratory Press
- Language
- English
- Date published
- 07/01/2005
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984293073002771
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