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Evolutionary design of glutathione-linked proteins in vivo and in vitro based on sampling of modules from pre-existing structures
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology.
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2001 (English)In: CHEMICO-BIOLOGICAL INTERACTIONS, ISSN 0009-2797, Vol. 133, no 1-3, 3-6 p.Article in journal (Refereed) Published
Abstract [en]

Structural studies suggest that naturally occurring proteins represent a limited number of folds. It would appear that the evolution of novel protein functions to a large extent involves redesign of stable peptide scaffolds by means of combinatorial prote

Place, publisher, year, edition, pages
ELSEVIER SCI IRELAND LTD , 2001. Vol. 133, no 1-3, 3-6 p.
Keyword [en]
combinatorial protein chemistry; glyoxalases; protein design; structural modules; HIGH CATALYTIC EFFICIENCY; HUMAN GLYOXALASE; LIPID-PEROXIDATION; CRYSTAL-STRUCTURE; GENE DUPLICATION; TRANSFERASES; SPECIFICITIES; DETOXICATION; PRODUCTS
Identifiers
URN: urn:nbn:se:uu:diva-38023OAI: oai:DiVA.org:uu-38023DiVA: diva2:65922
Note
Addresses: Mannervik B, Uppsala Univ, Dept Biochem, Ctr Biomed, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Dept Biochem, Ctr Biomed, SE-75123 Uppsala, Sweden. Uppsala Univ, Dept Mol Biol, SE-75123 Uppsala, Sweden.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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