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The ice-binding site of sea raven antifreeze protein is distinct from the carbohydrate-binding site of the homologous C-type lectin

Loewen, M. C., Gronwald, Wolfram, Sonnichsen, F. D., Sykes, B. D. and Davies, P. L. (1998) The ice-binding site of sea raven antifreeze protein is distinct from the carbohydrate-binding site of the homologous C-type lectin. Biochemistry 37 (51), pp. 17745-17753.

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Other URL: http://pubs.acs.org/doi/pdf/10.1021/bi9820513


Abstract

Antifreeze proteins lower the freezing point of their solution by binding to ice and inhibiting its growth. One of several structurally different antifreeze proteins in fishes (type II) is homologous to the carbohydrate-recognition domain of Ca2+-dependent lectins and adopts the same three-dimensional fold. Type II antifreeze proteins from herring and smelt require Ca2+ for binding to ice, ...

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Item type:Article
Date:22 December 1998
Institutions:Medicine > Institut für Funktionelle Genomik > Lehrstuhl für Funktionelle Genomik (Prof. Oefner)
Identification Number:
ValueType
9922140PubMed ID
10.1021/bi9820513DOI
Dewey Decimal Classification:600 Technology > 610 Medical sciences Medicine
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:No
Item ID:34354
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