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. 1993 Feb 19;259(5098):1154-7.
doi: 10.1126/science.8438165.

The nonhelical structure of antifreeze protein type III

F D Sönnichsen  1 , B D Sykes, H Chao, P L Davies
Affiliations

The nonhelical structure of antifreeze protein type III

F D Sönnichsen et al. Science. .

Abstract

Antifreeze proteins (AFPs) are present in the blood of some marine fishes and inhibit the growth of ice crystals at subzero temperatures by adsorption to the ice lattice. The solution structure of a Type III AFP was determined by two-dimensional nuclear magnetic resonance spectroscopy. These measurements indicate that this 66-residue protein has an unusual fold in which eight beta strands form two sheets of three antiparallel strands and one sheet of two antiparallel strands, and the triple-stranded sheets are packed orthogonally into a beta sandwich. This structure is completely different from the amphipathic, helical structure observed for Type I AFPs.

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