at Google ScholarTitle data
Höcker, Birte ; Jürgens, Catharina ; Wilmanns, Matthias ; Sterner, Reinhard:
Stability, catalytic versatility and evolution of the (betaalpha)(8)-barrel fold.
In: Current Opinion in Biotechnology.
Vol. 12
(2001)
Issue 4
.
- pp. 376-381.
ISSN 1879-0429
DOI: https://doi.org/10.1016/S0958-1669(00)00230-5
Abstract in another language
The (beta alpha)(8)-barrel is a versatile single-domain protein fold that is adopted by a large number of enzymes. The (beta alpha)(8)-barrel fold has been used as a model to elucidate the structural basis of protein thermostability and in studies to interconvert catalytic activities or substrate specificities by rational design or directed evolution. Recently, the (beta alpha)(4)-half-barrel was identified as a possible structural subdomain.
Further data
| Item Type: | Article in a journal |
|---|---|
| Refereed: | Yes |
| Institutions of the University: | Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Birte Höcker 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 > Chair Biochemistry |
| Result of work at the UBT: | No |
| DDC Subjects: | 500 Science > 540 Chemistry |
| Date Deposited: | 01 Jun 2017 10:12 |
| Last Modified: | 27 Oct 2022 10:28 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/37233 |