Nature of the early folding intermediate of ribonuclease A

Udgaonkar, Jayant B. ; Baldwin, Robert L. (1995) Nature of the early folding intermediate of ribonuclease A Biochemistry, 34 (12). pp. 4088-4096. ISSN 0006-2960

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A previous study of the folding pathway of the major unfolded species of ribonuclease A by pulsed hydrogen exchange [Udgaonkar, J.B., and Baldwin, R.L. (1990) Proc. Natl. Acad. Sco. U.S.A. 87, 8197-8201] showed that there is a major early folding intermediate (I1) that resembles a molten globule species in having stable secondary structure while lacking buried tyrosine side chains. Earlier work showed that there is also a late native-like folding intermediate (IN) that can bind the specific inhibitor 2'CMP and that has buried tyrosine side chains. Results are reported here indicating that I1 has a well-developed teriary structure even though its tyroside side chains are not buried. First, optical stopped-flow experimentes suggest that I1 binds 2'CMP. Second, the protection against hydrogen exchange is similar in I1 and IN for almost all protected amide protons studied. Third, analysis of the mechanism of hydrogen exchange in I1 confirms the large protection factors reported earlier for probes in the β-sheet of ribonuclease A and indicated that β-sheet is formed in I1. Other experiments are also reported that test the interpretation of pulsed hydrogen exchange studies of the folding pathway of ribonuclease A.

Item Type:Article
Source:Copyright of this article belongs to American Chemical Society.
ID Code:54325
Deposited On:11 Aug 2011 11:12
Last Modified:11 Aug 2011 11:12

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