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Updated: Aug 7, 2026

LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations
Published on: February 4, 2013
Structure-function relationship in the antifreeze activity of synthetic alanine-lysine antifreeze polypeptides
A Wierzbicki1, C A Knight, T J Rutland
1Department of Chemistry, University of South Alabama, Mobile, Alabama 36688, USA.
Abstract:
Recently antifreeze proteins (AFP) have been the subject of many structure-function relationship studies regarding their antifreeze activity. Attempts have been made to elucidate the structure-function relationship by various amino acid substitutions, but to our knowledge there has been no successful from first principles design of a polypeptide that would bind to designated ice planes along a specific direction. In this paper we show the results of our first attempt on an entirely de novo design of an alanine-lysine-rich antifreeze polypeptide. This 43 residue alanine-lysine peptide exhibits characteristic nonequilibrium freezing point depression and binds to the designated (210) planes of ice along the [122] vector. The structural and thermodynamic properties of this polypeptide were determined using circular dichroism spectroscopy and its nonequilibrium antifreeze properties were investigated using an ice-etching method and nanoliter osmometry.
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