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- W2042220007 abstract "The alanine-rich alpha-helical antifreeze protein from the winter flounder Pseudopleuronectes americanus adsorbs to specific planes of ice guided by an ice lattice match to threonine residues regularly spaced 16.6 A apart. We report here that by redesigning the winter flounder antifreeze peptide to incorporate a 27.1-A spacing between putative 'ice-binding' threonines, the deduced binding alignment of the helical molecule on the ice lattice is changed from the Miller indices directional vector [1102 ] to [2203 ]. Subsequent ice-binding characteristics are altered, including changes in adsorption specificity, decreases in thermal hysteresis activity and the formation of rotated hexagonal bipyramid ice crystal morphology." @default.
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- W2042220007 date "2002-01-01" @default.
- W2042220007 modified "2023-10-18" @default.
- W2042220007 title "Rational design of alpha-helical antifreeze peptides" @default.
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- W2042220007 doi "https://doi.org/10.1046/j.1397-002x.2001.00001.x" @default.
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