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Solution structure of a hydrophobic analogue of the winter flounder antifreeze protein

Liepinsh, Edvards; Harding, Margaret; Ward, Leanne G; Mackay, Joel Peter; Haymet, A D J; Otting, Gottfried

Description

The solution structure of a synthetic mutant type I antifreeze protein (AFP I) was determined in aqueous solution at pH 7.0 using nuclear magnetic resonance (NMR) spectroscopy. The mutations comprised the replacement of the four Thr residues by Val and the introduction of two additional Lys-Glu salt bridges. The antifreeze activity of this mutant peptide, VVVV2KE, has been previously shown to be similar to that of the wild type protein, HPLC6 (defined here as TTTT). The solution structure...[Show more]

dc.contributor.authorLiepinsh, Edvards
dc.contributor.authorHarding, Margaret
dc.contributor.authorWard, Leanne G
dc.contributor.authorMackay, Joel Peter
dc.contributor.authorHaymet, A D J
dc.contributor.authorOtting, Gottfried
dc.date.accessioned2015-12-13T22:26:29Z
dc.identifier.issn0014-2956
dc.identifier.urihttp://hdl.handle.net/1885/73530
dc.description.abstractThe solution structure of a synthetic mutant type I antifreeze protein (AFP I) was determined in aqueous solution at pH 7.0 using nuclear magnetic resonance (NMR) spectroscopy. The mutations comprised the replacement of the four Thr residues by Val and the introduction of two additional Lys-Glu salt bridges. The antifreeze activity of this mutant peptide, VVVV2KE, has been previously shown to be similar to that of the wild type protein, HPLC6 (defined here as TTTT). The solution structure reveals an ahelix bent in the same direction as the more bent conformer of the published crystalstructure of TTTT, while the side chain χ1 rotamers of VVVV2KE are similar to those of the straighter conformer in the crystal of TTTT. The Val side chains of VVVV2KE assume the same orientations as the Thr side chains of TTTT, confirming the conservative nature of this mutation. The combined data suggest that AFP I undergoes an equilibrium between straight and bent helices in solution, combined with independent equilibria between different side chain rotamers for some of the amino acid residues. The present study presents the first complete sequence-specific resonance assignments and the first complete solution structure determination by NMR of any AFP I protein.
dc.publisherBlackwell Publishing Ltd
dc.sourceEuropean Journal of Biochemistry
dc.subjectKeywords: antifreeze protein; glucose; lysine; threonine; valine; alpha helix; aqueous solution; article; crystal structure; flounder; mutant; mutation; nuclear magnetic resonance spectroscopy; pH; priority journal; protein structure; structure activity relation; A a helices; Antifreeze; NMR spectroscopy; Proteins; Winter flounder
dc.titleSolution structure of a hydrophobic analogue of the winter flounder antifreeze protein
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume269
dc.date.issued2002
local.identifier.absfor030400 - MEDICINAL AND BIOMOLECULAR CHEMISTRY
local.identifier.ariespublicationf5625xPUB3728
local.type.statusPublished Version
local.contributor.affiliationLiepinsh, Edvards, Karolinska Institute
local.contributor.affiliationOtting, Gottfried, Karolinska Institute
local.contributor.affiliationHarding, Margaret, Administrative Division, ANU
local.contributor.affiliationWard, Leanne G, University of Sydney
local.contributor.affiliationMackay, Joel Peter, University of Sydney
local.contributor.affiliationHaymet, A D J, University of Houston
local.description.embargo2037-12-31
local.bibliographicCitation.issue4
local.bibliographicCitation.startpage1259
local.bibliographicCitation.lastpage1266
local.identifier.doi10.1046/j.1432-1033.2002.02766.x
dc.date.updated2015-12-11T08:22:34Z
local.identifier.scopusID2-s2.0-0036177164
CollectionsANU Research Publications

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