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A conserved "hydrophobic staple motif" plays a crucial role in the refolding of human glutathione transferase P1-1
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
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2000 (English)In: JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, Vol. 275, no 14, 10421-10428 p.Article in journal (Refereed) Published
Abstract [en]

The specific (i, i+5) hydrophobic staple interaction involving a helix residue and a second residue located in the turn preceding the helix is a recurrent motif at the N terminus of alpha-helices, This motif is strictly conserved in the core of all solubl

Place, publisher, year, edition, pages
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC , 2000. Vol. 275, no 14, 10421-10428 p.
Keyword [en]
N-CAPPING BOX; S-TRANSFERASE; 3-DIMENSIONAL STRUCTURE; ALPHA-HELICES; PROTEINS; MECHANISM; IDENTIFICATION; ISOENZYMES; RESOLUTION; STABILITY
Identifiers
URN: urn:nbn:se:uu:diva-37998OAI: oai:DiVA.org:uu-37998DiVA: diva2:65897
Note
Addresses: Aceto A, Univ Chieti, Dipartimento Sci Biomed, Via Vestini 31, I-66100 Chieti, Italy. Univ Chieti, 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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