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.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Wierzbicki A,Knight CA,Rutland TJ,Muccio DD,Pybus BS,Sikes CSdoi
10.1021/bm000004wkeywords:
subject
Has Abstractpub_date
2000-07-01 00:00:00pages
268-74issue
2eissn
1525-7797issn
1526-4602journal_volume
1pub_type
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