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Valine substituted winter flounder 'antifreeze': preservation of ice growth hysteresis

Haymet, A D J; Ward, Leanne G; Harding, Margaret; Knight, Charles A

Description

Three mutant polypeptides of the type 1 37-residue winter flounder 'antifreeze' protein have been synthesized. All four threonine residues in the native peptide were been mutated to serine, valine and glycine respectively and two additional salt bridges were incorporated into the sequences in order to improve aqueous solubility. The peptides were analyzed by nanoliter osmometry, the 'ice hemisphere' test, the 'crystal habit' test, measurement of ice growth hysteresis and CD spectroscopy. While...[Show more]

dc.contributor.authorHaymet, A D J
dc.contributor.authorWard, Leanne G
dc.contributor.authorHarding, Margaret
dc.contributor.authorKnight, Charles A
dc.date.accessioned2015-12-13T22:26:21Z
dc.identifier.issn0014-5793
dc.identifier.urihttp://hdl.handle.net/1885/73481
dc.description.abstractThree mutant polypeptides of the type 1 37-residue winter flounder 'antifreeze' protein have been synthesized. All four threonine residues in the native peptide were been mutated to serine, valine and glycine respectively and two additional salt bridges were incorporated into the sequences in order to improve aqueous solubility. The peptides were analyzed by nanoliter osmometry, the 'ice hemisphere' test, the 'crystal habit' test, measurement of ice growth hysteresis and CD spectroscopy. While the valine and serine mutants retain the α-helical structure, only the valine mutant retains 'antifreeze' activity similar to that of the native protein. These data show that the threonine hydroxyl groups do not play a crucial role in the accumulation of the native 'antifreeze' protein at the ice/water interface and the inhibition of ice growth below the equilibrium melting temperature.
dc.publisherElsevier
dc.sourceFEBS Letters
dc.subjectKeywords: antifreeze protein; glycine; ice; mutant protein; serine; sodium chloride; threonine; valine; amino acid substitution; aqueous solution; article; circular dichroism; flounder; hysteresis; nonhuman; peptide synthesis; priority journal; solubility; winter; a-Helical peptide; Antifreeze; Hysteresis; Ice growth inhibition; Threonine residue
dc.titleValine substituted winter flounder 'antifreeze': preservation of ice growth hysteresis
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume430
dc.date.issued1998
local.identifier.absfor060100 - BIOCHEMISTRY AND CELL BIOLOGY
local.identifier.ariespublicationf5625xPUB3709
local.type.statusPublished Version
local.contributor.affiliationHaymet, A D J, University of Houston
local.contributor.affiliationWard, Leanne G, University of Sydney
local.contributor.affiliationHarding, Margaret, Administrative Division, ANU
local.contributor.affiliationKnight, Charles A, National Center for Atmospheric Research
local.description.embargo2037-12-31
local.bibliographicCitation.issue3
local.bibliographicCitation.startpage301
local.bibliographicCitation.lastpage306
local.identifier.doi10.1016/s0014-5793(98)00652-8
dc.date.updated2015-12-11T08:21:48Z
local.identifier.scopusID2-s2.0-0032479347
CollectionsANU Research Publications

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