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Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding

Title data

Kiefhaber, Thomas ; Grunert, Hans Peter ; Hahn, Ulrich ; Schmid, Franz X.:
Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding.
In: Biochemistry. Vol. 29 (10 July 1990) Issue 27 . - pp. 6475-6480.
ISSN 0006-2960
DOI: https://doi.org/10.1021/bi00479a020

Abstract in another language

The refolding of ribonuclease T1 is dominated by two major slow kinetic phases that show properties of proline isomerization reactions. We report here that the molecular origin of one of these processes is the trans----cis isomerization of the Ser54-Pro55 peptide bond, which is cis in the native protein but predominantly trans in unfolded ribonuclease T1. This is shown by a comparison of the wild type and a designed mutant protein where Ser54 and Pro55 were replaced by Gly54 and Asn55, respectively. This mutation leaves the thermal stability of the protein almost unchanged; however, in the absence of Pro55 one of the two slow phases in folding is abolished and the kinetic mechanism of refolding is dramatically simplified.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 2119802
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: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 12 May 2015 08:21
Last Modified: 12 May 2015 08:21
URI: https://eref.uni-bayreuth.de/id/eprint/13295