at Google ScholarTitle data
Schmid, Franz X. ; Frech, Christian ; Scholz, Christian ; Walter, Stefan:
Catalyzed and assisted protein folding of ribonuclease T1.
In: Biological Chemistry.
Vol. 377
(1996)
Issue 7-8
.
- pp. 417-424.
ISSN 1437-4315
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 > 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: | 18 May 2015 07:12 |
| Last Modified: | 21 Apr 2022 13:44 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/13516 |