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Denaturation configurational entropy change

At this temperature, the entropy change for dissolution of liquid hydrocarbons in water is zero. However, the entropy of protein denaturation is far from zero at this temperature but amounts to 17.6 J - K l per mole of amino acid residues (Privalov, 1979), a value that corresponds to an 8-fold increase of the number of possible configurations and is close to the value expected for the helix-coil transition of polypeptides (Schellman, 1955). This difference shows that an oil drop is an inadequate model for a globular protein. A more suitable model resembles that of a small crystal with a quite definite positive melting entropy (see also Bellow, 1977, 1978). [Pg.225]


See other pages where Denaturation configurational entropy change is mentioned: [Pg.337]    [Pg.338]    [Pg.339]    [Pg.180]    [Pg.292]    [Pg.318]    [Pg.183]    [Pg.266]    [Pg.142]    [Pg.2841]    [Pg.41]    [Pg.2841]    [Pg.142]    [Pg.145]    [Pg.603]   
See also in sourсe #XX -- [ Pg.180 ]




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