Solution structure of a hydrophobic analogue of the winter flounder antifreeze protein
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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.author | Liepinsh, Edvards | |
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dc.contributor.author | Harding, Margaret | |
dc.contributor.author | Ward, Leanne G | |
dc.contributor.author | Mackay, Joel Peter | |
dc.contributor.author | Haymet, A D J | |
dc.contributor.author | Otting, Gottfried | |
dc.date.accessioned | 2015-12-13T22:26:29Z | |
dc.identifier.issn | 0014-2956 | |
dc.identifier.uri | http://hdl.handle.net/1885/73530 | |
dc.description.abstract | 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 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.publisher | Blackwell Publishing Ltd | |
dc.source | European Journal of Biochemistry | |
dc.subject | Keywords: 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.title | Solution structure of a hydrophobic analogue of the winter flounder antifreeze protein | |
dc.type | Journal article | |
local.description.notes | Imported from ARIES | |
local.identifier.citationvolume | 269 | |
dc.date.issued | 2002 | |
local.identifier.absfor | 030400 - MEDICINAL AND BIOMOLECULAR CHEMISTRY | |
local.identifier.ariespublication | f5625xPUB3728 | |
local.type.status | Published Version | |
local.contributor.affiliation | Liepinsh, Edvards, Karolinska Institute | |
local.contributor.affiliation | Otting, Gottfried, Karolinska Institute | |
local.contributor.affiliation | Harding, Margaret, Administrative Division, ANU | |
local.contributor.affiliation | Ward, Leanne G, University of Sydney | |
local.contributor.affiliation | Mackay, Joel Peter, University of Sydney | |
local.contributor.affiliation | Haymet, A D J, University of Houston | |
local.description.embargo | 2037-12-31 | |
local.bibliographicCitation.issue | 4 | |
local.bibliographicCitation.startpage | 1259 | |
local.bibliographicCitation.lastpage | 1266 | |
local.identifier.doi | 10.1046/j.1432-1033.2002.02766.x | |
dc.date.updated | 2015-12-11T08:22:34Z | |
local.identifier.scopusID | 2-s2.0-0036177164 | |
Collections | ANU Research Publications |
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