Titlebar

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

 

Stability, catalytic versatility and evolution of the (betaalpha)(8)-barrel fold

Title 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 (August 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: 01 Jun 2017 10:12
URI: https://eref.uni-bayreuth.de/id/eprint/37233