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Stabilisation of a (betaalpha)8-barrel protein designed from identical half barrels.

Seitz, Tobias, Bocola, Marco, Claren, Jörg and Sterner, Reinhard (2007) Stabilisation of a (betaalpha)8-barrel protein designed from identical half barrels. Journal of molecular biology 372 (1), pp. 114-29.

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Abstract

It has been suggested that the common (betaalpha)(8)-barrel enzyme fold has evolved by the duplication and fusion of identical (betaalpha)(4)-half barrels, followed by the optimisation of their interface. In our attempts to reconstruct these events in vitro we have previously linked in tandem two copies of the C-terminal half barrel HisF-C of imidazole glycerol phosphate synthase from Thermotoga ...

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Item type:Article
Date:2007
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
17631894PubMed ID
10.1016/j.jmb.2007.06.036DOI
Classification:
NotationType
Aminohydrolases/geneticsMESH
Computer SimulationMESH
Enzyme Stability/geneticsMESH
Histidine/chemistryMESH
Models, BiologicalMESH
Models, MolecularMESH
Mutagenesis, Site-DirectedMESH
Protein DenaturationMESH
Protein FoldingMESH
Protein Structure, TertiaryMESH
SolubilityMESH
Thermotoga maritima/geneticsMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:13672
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