rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
1423
|
pubmed:dateCreated |
2002-8-12
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pubmed:abstractText |
High-resolution three-dimensional structures are now available for four of seven non-homologous fish and insect antifreeze proteins (AFPs). For each of these structures, the ice-binding site of the AFP has been defined by site-directed mutagenesis, and ice etching has indicated that the ice surface is bound by the AFP. A comparison of these extremely diverse ice-binding proteins shows that they have the following attributes in common. The binding sites are relatively flat and engage a substantial proportion of the protein's surface area in ice binding. They are also somewhat hydrophobic -- more so than that portion of the protein exposed to the solvent. Surface-surface complementarity appears to be the key to tight binding in which the contribution of hydrogen bonding seems to be secondary to van der Waals contacts.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12171656-10437807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12171656-10601644,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12171656-9756474
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
0962-8436
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
29
|
pubmed:volume |
357
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
927-35
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
|
pubmed:year |
2002
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pubmed:articleTitle |
Structure and function of antifreeze proteins.
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pubmed:affiliation |
Department of Biochemistry, Queen's University, Kingston, Ontario, Canada K7L 3N6. daviesp@post.queensu.ca
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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