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

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.

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Abstract

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.

Item Type:Article
Institutions: Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
11551466PubMed ID
Classification:
NotationType
CatalysisMESH
Directed Molecular Evolution/methodsMESH
Evolution, MolecularMESH
Phosphopyruvate Hydratase/metabolismMESH
Protein FoldingMESH
Protein Structure, SecondaryMESH
Substrate SpecificityMESH
ThermodynamicsMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Owner:Universitätsbibliothek Regensburg
Deposited On:22 Mar 2010 09:43
Last Modified:22 Mar 2010 09:43
Item ID:13696
Owner Only: item control page