Document Detail

A diminished role for hydrogen bonds in antifreeze protein binding to ice.
MedLine Citation:
PMID:  9398184     Owner:  NLM     Status:  MEDLINE    
The most abundant isoform (HPLC-6) of type I antifreeze protein (AFP1) in winter flounder is a 37-amino-acid-long, alanine-rich, alpha-helical peptide, containing four Thr spaced 11 amino acids apart. It is generally assumed that HPLC-6 binds ice through a hydrogen-bonding match between the Thr and neighboring Asx residues to oxygens atoms on the {2021} plane of the ice lattice. The result is a lowering of the nonequilibrium freezing point below the melting point (thermal hysteresis). HPLC-6, and two variants in which the central two Thr were replaced with either Ser or Val, were synthesized. The Ser variant was virtually inactive, while only a minor loss of activity was observed in the Val variant. CD, ultracentrifugation, and NMR studies indicated no significant structural changes or aggregation of the variants compared to HPLC-6. These results call into question the role of hydrogen bonds and suggest a much more significant role for entropic effects and van der Waals interactions in binding AFP to ice.
H Chao; M E Houston; R S Hodges; C M Kay; B D Sykes; M C Loewen; P L Davies; F D Sönnichsen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  36     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1997 Dec 
Date Detail:
Created Date:  1998-01-08     Completed Date:  1998-01-08     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  14652-60     Citation Subset:  IM    
Protein Engineering Network of Centres of Excellence, University of Alberta, Edmonton, Canada.
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MeSH Terms
Amino Acid Sequence
Antifreeze Proteins
Centrifugation, Isopycnic
Circular Dichroism
Glycoproteins / chemistry,  metabolism*
Hydrogen Bonding
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
Serine / chemistry,  metabolism
Threonine / chemistry,  metabolism
Valine / chemistry,  metabolism
Grant Support
Reg. No./Substance:
0/Antifreeze Proteins; 0/Glycoproteins; 0/Ice; 56-45-1/Serine; 7004-03-7/Valine; 72-19-5/Threonine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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