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High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels.

Höcker, Birte and Lochner, Adriane and Seitz, Tobias and Claren, Jörg and Sterner, Reinhard (2009) High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels. Biochemistry 48 (6), pp. 1145-7.

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Abstract

Ample evidence suggests that the ubiquitous (betaalpha)(8)-barrel enzyme fold has evolved by the duplication and fusion of an ancestral (betaalpha)(4)-half-barrel. To reconstruct this process in the laboratory with a model protein, we earlier fused two copies of the C-terminal half-barrel HisF-C of imidazole glycerol phosphate synthase (HisF) and stepwise stabilized the resulting HisF-CC ...

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Item Type:Article
Date:2009
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
19166324PubMed ID
10.1021/bi802125bDOI
Classification:
NotationType
Aminohydrolases/chemistryMESH
Crystallography, X-RayMESH
Protein Structure, SecondaryMESH
Recombinant Proteins/chemistryMESH
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 07:24
Last Modified:22 Mar 2010 07:24
Item ID:13666
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