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A conserved 'hydrophobic staple motif' plays a crucial role in the refolding of human glutathione transferase Pl-l
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
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2001 (English)In: CHEMICO-BIOLOGICAL INTERACTIONS, ISSN 0009-2797, Vol. 133, no 1-3, 49-50 p.Article in journal (Refereed) Published
Abstract [en]

A hydrophobic staple motif is strictly conserved in the core of all soluble glutathione transferases (GSTs) as well as in other protein structures. The role of this local interaction in folding and stability of human GSTP1-1 has been analysed by site dire

Place, publisher, year, edition, pages
ELSEVIER SCI IRELAND LTD , 2001. Vol. 133, no 1-3, 49-50 p.
Keyword [en]
hGSTP1-1; folding; hydrophobic staple motif; interdomain interactions
URN: urn:nbn:se:uu:diva-38040OAI: oai:DiVA.org:uu-38040DiVA: diva2:65939
Addresses: Aceto A, Univ G DAnnunzio, Dipartimento Sci Biomed, Via Vestini 31, I-66100 Chieti, Italy. Univ G DAnnunzio, Dipartimento Sci Biomed, I-66100 Chieti, Italy. Univ Uppsala, Ctr Biomed, Dept Biochem, S-75123 Uppsala, Sweden.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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