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Allosteric proteins hydrophobic association

Identification of Hydrophobic Association with Rigor in Muscle and with the Tense, T-State, of Allosteric Proteins Exhibiting Positive Cooperativity... [Pg.243]

Ca2+ influx initiates protein and membrane associations by several different mechanisms. Allosteric regulation of the hydrophobicity of protein-binding surfaces frequently occurs. One of the best studied examples is the Ca2+-dependent binding of calmodulin to other proteins (Ch. 22). Annexins are a family of proteins that exhibit Ca2+-dependent associations with cell membranes through direct interaction with phospholipids, and conversely, interactions with phospholipids increase their affinities for Ca2+ [7]. [Pg.25]


See other pages where Allosteric proteins hydrophobic association is mentioned: [Pg.141]    [Pg.196]    [Pg.243]    [Pg.183]    [Pg.379]    [Pg.232]    [Pg.385]    [Pg.386]    [Pg.400]   


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Allosterism

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Protein , association

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