| pubmed-article:12171656 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12171656 | lifeskim:mentions | umls-concept:C0103575 | lld:lifeskim |
| pubmed-article:12171656 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:12171656 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12171656 | pubmed:issue | 1423 | lld:pubmed |
| pubmed-article:12171656 | pubmed:dateCreated | 2002-8-12 | lld:pubmed |
| pubmed-article:12171656 | 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. | lld:pubmed |
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| pubmed-article:12171656 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12171656 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12171656 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12171656 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12171656 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12171656 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:12171656 | pubmed:issn | 0962-8436 | lld:pubmed |
| pubmed-article:12171656 | pubmed:author | pubmed-author:DaviesPeter... | lld:pubmed |
| pubmed-article:12171656 | pubmed:author | pubmed-author:WalkerVirgini... | lld:pubmed |
| pubmed-article:12171656 | pubmed:author | pubmed-author:BaardsnesJaso... | lld:pubmed |
| pubmed-article:12171656 | pubmed:author | pubmed-author:KuiperMichael... | lld:pubmed |
| pubmed-article:12171656 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12171656 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:12171656 | pubmed:volume | 357 | lld:pubmed |
| pubmed-article:12171656 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12171656 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12171656 | pubmed:pagination | 927-35 | lld:pubmed |
| pubmed-article:12171656 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12171656 | pubmed:meshHeading | pubmed-meshheading:12171656... | lld:pubmed |
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| pubmed-article:12171656 | pubmed:meshHeading | pubmed-meshheading:12171656... | lld:pubmed |
| pubmed-article:12171656 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12171656 | pubmed:articleTitle | Structure and function of antifreeze proteins. | lld:pubmed |
| pubmed-article:12171656 | pubmed:affiliation | Department of Biochemistry, Queen's University, Kingston, Ontario, Canada K7L 3N6. daviesp@post.queensu.ca | lld:pubmed |
| pubmed-article:12171656 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12171656 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:12171656 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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