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Control of protein function by prolyl isomerization.

Title data

Schmidpeter, Philipp A. M. ; Koch, Johanna R. ; Schmid, Franz X.:
Control of protein function by prolyl isomerization.
In: Biochimica et Biophysica Acta : General Subjects. (24 December 2014) .
ISSN 1872-8006
DOI: https://doi.org/10.1016/j.bbagen.2014.12.019

Abstract in another language

Background: Prolyl cis/trans isomerizations have long been known as critical and rate-limiting steps in protein folding. Results: Now it is clear that they are also used as slow conformational switches and molecular timers in the regulation of protein activity. Here we describe several such proline switches and how they are regulated. Conclusions and general significance: Prolyl isomerizations can function as attenuators and provide allosteric systems with a molecular memory.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 25542300
Institutions of the University: 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 > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
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: 21 Apr 2015 13:01
Last Modified: 22 Apr 2015 07:02
URI: https://eref.uni-bayreuth.de/id/eprint/10463