Crystallography reveals secrets of nature's antifreeze - physicsworld.com
Crystallography reveals secrets of nature's antifreeze physicsworld.com
Ansgar Siemer of Columbia University in New York City, who has used nuclear magnetic resonance (NMR) to identify the ice-binding sites on antifreeze proteins, believes this detailed picture of the protein's structure will be useful to researchers. ...
Crystallography reveals secrets of nature's antifreeze - physicsworld.com More...
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Proteins Reveal Their Secrets Under Pressure
Chemical & Engineering News
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NMR characterizations of the ice binding surface of an antifreeze protein.
NMR characterizations of the ice binding surface of an antifreeze protein.
NMR characterizations of the ice binding surface of an antifreeze protein.
PLoS One. 2010;5(12):e15682
Authors: Hong J, Hu Y, Li C, Jia Z, Xia B, Jin C
Antifreeze protein (AFP) has a unique function of reducing solution freezing temperature to protect organisms from ice damage. However, its functional mechanism is not well understood. An intriguing question concerning AFP function is how the high selectivity for ice ligand is achieved in the presence of free water of...
nmrlearner
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01-07-2011 11:21 PM
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The dependence of amide proton chemical shifts on temperature is used as an indication of the hydrogen bonding properties in a protein. The amide proton temperature coefficients of the beta-helical...
nmrlearner
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11-24-2010 09:51 PM
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Biochem Cell Biol. 1998;76(2-3):284-93
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Antifreeze proteins (AFPs) are a structurally diverse class of proteins that bind to ice and inhibit its growth in a noncolligative manner. This adsorption-inhibition mechanism operating at the ice surface results in a lowering of the (nonequilibrium) freezing point below the melting point. A lowering of approximately 1 degree C, which is sufficient to...