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

Abstract:

:Three mutant polypeptides of the type I 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 alpha-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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Haymet AD,Ward LG,Harding MM,Knight CA

doi

10.1016/s0014-5793(98)00652-8

subject

Has Abstract

pub_date

1998-07-03 00:00:00

pages

301-6

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)00652-8

journal_volume

430

pub_type

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