Höcker, Birte and Jürgens, Catharina and Wilmanns, Matthias and Sterner, Reinhard (2001) Stability, catalytic versatility and evolution of the (beta alpha)(8)-barrel fold. Current opinion in biotechnology 12 (4), pp. 376-81.
Full text not available from this repository.
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.
Export bibliographical data
|Institutions:||Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner|
|Dewey Decimal Classification:||500 Science > 570 Life sciences|
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||Yes|
|Deposited On:||22 Mar 2010 08:43|
|Last Modified:||22 Mar 2010 08:43|