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
(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 > Professor 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: | 31 Mar 2022 13:18 |
URI: | https://eref.uni-bayreuth.de/id/eprint/13471 |