| Autor: |
Trefethen JM; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-1114, USA., Pace CN, Scholtz JM, Brems DN |
| Jazyk: |
angličtina |
| Zdroj: |
Protein science : a publication of the Protein Society [Protein Sci] 2005 Jul; Vol. 14 (7), pp. 1934-8. Date of Electronic Publication: 2005 Jun 03. |
| DOI: |
10.1110/ps.051401905 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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