By Jacinto Steinhardt
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Extra resources for Multiple Equilibria in Proteins
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Polet, and J. Steinhardt (1967). ] -6 -5 -4 -3 -2 -I Log C FIG. 2-4. 6 with various detergent sulfates. [J. Reynolds, S. Herbert, H. Polet, and J. Steinhardt (1967). ] 27 28 II THERMODYNAMICS AND MODEL SYSTEMS binding isotherm of sodium dodecylsulfate to bovine serum albumin (Fig. 0. By itself this does not prove conformational change in the protein since the large increase in binding over a relatively narrow range in C e q could also be caused by micelle formation. ") However, taken together with the viscosity and optical data, the singularity in the binding isotherm in this specific case is recognized as due to massive unfolding of the protein which leads to exposure of a large number of new sites with an association constant which may differ from that of the first set of sites on the native molecule.
Note that the FIG. 2-2. Viscosities (a) and specific rotation (b) of BSA-alkyl sulfonate complexes as a function of molal ratio v. (b) At Cotton effect trough (233 m/x). [J. Reynolds, S. Herbert, H. Polet, and J. Steinhardt (1967). ] FIG. 2-3. Spécifie viscosities (a) and specific rotation (b) of various BSA-detergent sulfate complexes as a function of molal ratio v. (b) At the Cotton effect trough (233 m/x). The insert shows results with dodecylsulfate 546 m/x. [J. Reynolds, S. Herbert, H. Polet, and J.