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Stability, catalytic versatility and evolution of the (beta alpha)(8)-barrel fold.

Höcker, Birte, Jürgens, Catharina, 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.

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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.

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Item type:Article
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
11551466PubMed ID
Directed Molecular Evolution/methodsMESH
Evolution, MolecularMESH
Phosphopyruvate Hydratase/metabolismMESH
Protein FoldingMESH
Protein Structure, SecondaryMESH
Substrate SpecificityMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:13696
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