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Generation of a non-prolyl cis peptide bond in ribonuclease T1

Title data

Mayr, Lorenz M. ; Willbold, Dieter ; Rösch, Paul ; Schmid, Franz X.:
Generation of a non-prolyl cis peptide bond in ribonuclease T1.
In: Journal of Molecular Biology. Vol. 240 (22 July 1994) Issue 4 . - pp. 288-293.
ISSN 0022-2836
DOI: https://doi.org/10.1006/jmbi.1994.1446

Abstract in another language

The cis conformation of the 38-39 peptide bond of ribonuclease T1 is retained after the replacement of cis Pro39 by an alanine residue. This conformation is demonstrated by the presence of a NOESY cross-peak in the NMR spectrum between the C alpha protons of Tyr38 and Ala39 in the Pro39-->Ala variant. The presence of this non-prolyl cis peptide bond explains the retention of the catalytic activity, the strong decrease in stability and the changes in the folding mechanism that were observed after the Pro39-->Ala mutation in ribonuclease T1. We suggest that a cis peptide bond is retained in a protein after the substitution of a cis proline at positions, where a trans bond would destabilize the protein more strongly than a non-prolyl peptide bond in the energetically unfavourable cis conformation.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 8035456
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: 15 May 2015 05:48
Last Modified: 15 May 2015 05:48
URI: https://eref.uni-bayreuth.de/id/eprint/13471