Titlebar

Export bibliographic data
Literature by the same author
plus on the publication server
plus at Google Scholar

 

Proline isomerization in unfolded ribonuclease A : The equilibrium between fast-folding and slow-folding species is independent of temperature

Title data

Schmid, Franz X.:
Proline isomerization in unfolded ribonuclease A : The equilibrium between fast-folding and slow-folding species is independent of temperature.
In: European Journal of Biochemistry. Vol. 128 (November 1982) Issue 1 . - pp. 77-80.
ISSN 1432-1033
DOI: https://doi.org/10.1111/j.1432-1033.1982.tb06935.x

Official URL: Volltext

Related URLs

Abstract in another language

Unfolded ribonuclease A (RNaseA) consists of a mixture of fast refolding (UF) and slow-refolding (Us) species. The slow UF in equilibrium Us equilibration reaction is rate-limited by proline peptide bond isomerization. Investigations of the dependence on temperature of the UF in equilibrium Us equilibrium have led to conflicting results and different molecular interpretations. Here the dependence on temperature of the UF:US ratio was reinvestigated by using a new assay for the fast-folding molecules UF. Between 0 degrees C and 60 degrees C the proportion of UF present in unfolded RNase A at 6 M guanidine . HCl was found to be independent of temperature. Consequently, no conclusions can be drawn regarding the role and importance of particular prolines in the UF in equilibrium US transition solely from these results.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 7173213
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: 29 Apr 2015 11:59
Last Modified: 29 Apr 2015 11:59
URI: https://eref.uni-bayreuth.de/id/eprint/11210