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Catalyzed and assisted protein folding of ribonuclease T1

Title data

Schmid, Franz X. ; Frech, Christian ; Scholz, Christian ; Walter, Stefan:
Catalyzed and assisted protein folding of ribonuclease T1.
In: Biological Chemistry. Vol. 377 (August 1996) Issue 7-8 . - pp. 417-424.
ISSN 1431-6730

Abstract in another language

The small single-domain protein ribonuclease T1 (RNase T1) and variants thereof are good substrates for investigating the mechanisms of catalyzed and assisted protein folding. RNase T1 contains two cis prolines and two disulfide bonds, and the kinetic mechanism of its folding is well known. The wild-type form and designed variants that differ in the number prolines and of disulfide bonds were used as substrates to study the catalysis of folding by prolyl isomerases and protein disulfide isomerases. In its unfolded form, a marginally stable variant of RNase T1 binds to the chaperone GroEL and could thus be used to elucidate the kinetic mechanism of GroEL-mediated protein unfolding.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 8922275
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: 18 May 2015 07:12
Last Modified: 27 Apr 2016 12:00
URI: https://eref.uni-bayreuth.de/id/eprint/13516