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Solution Structure of a Recombinant Type I Sculpin Antifreeze Protein

Kwan, Ann H-Y; Fairley, Kayesh; Anderberg, Pia I; Liew, Chu W; Harding, Margaret; Mackay, Joel Peter

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We have determined the solution structure of rSS3, a recombinant form of the type I shorthorn sculpin antifreeze protein (AFP), at 278 and 268 K. This AFP contains an unusual sequence of N-terminal residues, together with two of the 11-residue repeats that are characteristic of the type I winter flounder AFP. The solution conformation of the N-terminal region of the sculpin AFP has been assumed to be the critical factor that results in recognition of different ice planes by the sculpin and...[Show more]

dc.contributor.authorKwan, Ann H-Y
dc.contributor.authorFairley, Kayesh
dc.contributor.authorAnderberg, Pia I
dc.contributor.authorLiew, Chu W
dc.contributor.authorHarding, Margaret
dc.contributor.authorMackay, Joel Peter
dc.date.accessioned2015-12-13T22:26:33Z
dc.identifier.issn0006-2960
dc.identifier.urihttp://hdl.handle.net/1885/73556
dc.description.abstractWe have determined the solution structure of rSS3, a recombinant form of the type I shorthorn sculpin antifreeze protein (AFP), at 278 and 268 K. This AFP contains an unusual sequence of N-terminal residues, together with two of the 11-residue repeats that are characteristic of the type I winter flounder AFP. The solution conformation of the N-terminal region of the sculpin AFP has been assumed to be the critical factor that results in recognition of different ice planes by the sculpin and flounder AFPs. At 278 K, the two repeats units (residues 11-20 and 21-32) in rSS3 form a continuous α-helix, with the residues 30-33 in the second repeat somewhat less well defined. Within the N-terminal region, residues 2-6 are well defined and helical and linked to the main helix by a more flexible region comprising residues A7-T11. At 268 K the AFP is overall more helical but retains the apparent hinge region. The helical conformation of the two repeats units is almost identical to the corresponding repeats in the type I winter flounder AFP. We also show that while tetracetylated rSS3 has antifreeze activity comparable to the natural AFP, its overall structure is the same as that of the unacetylated peptide. These data provide some insight into the structural determinants of antifreeze activity and should assist in the development of models that explain the recognition of different ice interfaces by the sculpin and flounder type I AFPs.
dc.publisherAmerican Chemical Society
dc.sourceBiochemistry
dc.subjectKeywords: Antifreeze solutions; Hinges; Ice; Mathematical models; Structural design; Tetrodes; Residues; Sculpin antifreeze protein (AFP); Solution structure; Terminal region; Proteins; antifreeze protein; ice; peptide derivative; protein rSS3; recombinant protein;
dc.titleSolution Structure of a Recombinant Type I Sculpin Antifreeze Protein
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume44
dc.date.issued2005
local.identifier.absfor060100 - BIOCHEMISTRY AND CELL BIOLOGY
local.identifier.ariespublicationf5625xPUB3737
local.type.statusPublished Version
local.contributor.affiliationKwan, Ann H-Y, University of Sydney
local.contributor.affiliationFairley, Kayesh, University of Sydney
local.contributor.affiliationAnderberg, Pia I, University of Sydney
local.contributor.affiliationLiew, Chu W, University of Sydney
local.contributor.affiliationHarding, Margaret, Administrative Division, ANU
local.contributor.affiliationMackay, Joel Peter, University of Sydney
local.description.embargo2037-12-31
local.bibliographicCitation.issue6
local.bibliographicCitation.startpage1980
local.bibliographicCitation.lastpage1988
local.identifier.doi10.1021/bi047782j
dc.date.updated2015-12-11T08:22:58Z
local.identifier.scopusID2-s2.0-13544268362
CollectionsANU Research Publications

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