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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2003-6-25
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pubmed:abstractText |
Two-dimensional nuclear magnetic resonance spectroscopy was used to investigate the flexibility of the threonine side chains in the beta-helical Tenebrio molitor antifreeze protein (TmAFP) at low temperatures. From measurement of the (3)J(alphabeta) (1)H-(1)H scalar coupling constants, the chi(1) angles and preferred rotamer populations can be calculated. It was determined that the threonines on the ice-binding face of the protein adopt a preferred rotameric conformation at near freezing temperatures, whereas the threonines not on the ice-binding face sample many rotameric states. This suggests that TmAFP maintains a preformed ice-binding conformation in solution, wherein the rigid array of threonines that form the AFP-ice interface matches the ice crystal lattice. A key factor in binding to the ice surface and inhibition of ice crystal growth appears to be the close surface-to-surface complementarity between the AFP and crystalline ice, and the lack of an entropic penalty associated with freezing out motions in a flexible ligand.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-10601644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-10833402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-10917518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-10917536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-10917537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-11159432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-11181959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-11181960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-11509380,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-11852248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-11969412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-12429502,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-1489916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-2009357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-2185972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-2676353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-267952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-6661238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-7664040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-7760940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-8988006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-9285581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-9398184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-9434903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-9565593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-9688560,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12824479-9857006
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1323-31
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12824479-Amino Acid Sequence,
pubmed-meshheading:12824479-Animals,
pubmed-meshheading:12824479-Antifreeze Proteins,
pubmed-meshheading:12824479-Crystallography, X-Ray,
pubmed-meshheading:12824479-Magnetic Resonance Spectroscopy,
pubmed-meshheading:12824479-Molecular Sequence Data,
pubmed-meshheading:12824479-Pliability,
pubmed-meshheading:12824479-Protein Conformation,
pubmed-meshheading:12824479-Protein Isoforms,
pubmed-meshheading:12824479-Solubility,
pubmed-meshheading:12824479-Temperature,
pubmed-meshheading:12824479-Tenebrio,
pubmed-meshheading:12824479-Threonine
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pubmed:year |
2003
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pubmed:articleTitle |
The role of side chain conformational flexibility in surface recognition by Tenebrio molitor antifreeze protein.
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pubmed:affiliation |
Canadian Institutes of Health Research (CIHR) Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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