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 Lettjournal_title
FEBS lettersauthors
Haymet AD,Ward LG,Harding MM,Knight CAdoi
10.1016/s0014-5793(98)00652-8subject
Has Abstractpub_date
1998-07-03 00:00:00pages
301-6issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(98)00652-8journal_volume
430pub_type
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