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

A. D.J. Haymet*, Leanne G. Ward, Margaret M. Harding, Charles A. Knight

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

148 Citations (Scopus)

Abstract

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 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.

Original languageEnglish
Pages (from-to)301-306
Number of pages6
JournalFEBS Letters
Volume430
Issue number3
DOIs
Publication statusPublished - 3 Jul 1998
Externally publishedYes

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