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An early intermediate in the folding of ribonuclease A is protected against cleavage by pepsin

Title data

Schmid, Franz X. ; Blaschek, Heidi:
An early intermediate in the folding of ribonuclease A is protected against cleavage by pepsin.
In: Biochemistry. Vol. 23 (8 May 1984) Issue 10 . - pp. 2128-2133.
ISSN 0006-2960
DOI: https://doi.org/10.1021/bi00305a004

Abstract in another language

Folding of bovine pancreatic ribonuclease A (RNase A) is a sequential process which involves the formation of well-populated structural intermediates under suitable conditions. Two intermediates have been detected on the major slow-refolding pathway of RNase A: a late intermediate (IN) which already resembles the native protein in a number of properties and a rapidly formed early intermediate (I1) which shows extensive hydrogen-bonded secondary structure. Here competition experiments between refolding and proteolytic cleavage of the peptide chain are described which yield information about the decrease in accessibility of particular proteolytic cleavage sites during the folding process. Results obtained with pepsin as a proteolytic probe of folding indicate that the primary cleavage site for pepsin, Phe-120-Asp-121, becomes inaccessible early in the course of refolding, if folding is carried out under conditions which effectively stabilize the native state. Under marginally stable conditions, folding is very slow, and protection against peptic cleavage is not detectable prior to the final formation of native protein. The comparison with amide proton exchange experiments suggests that the protection against peptic cleavage occurs during the formation and/or stabilization of hydrogen-bonded secondary structure in the early intermediate (I1). We conclude that the carboxy-terminal region of the RNase peptide chain, which is known to be important for the stability of the folded protein, may also be relevant for early steps of refolding.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 6428447
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 12 May 2015 06:39
Last Modified: 12 May 2015 06:39
URI: https://eref.uni-bayreuth.de/id/eprint/13289