| Abstract: | The effectiveness of a variety of protein denaturants has been determined on two proteins, [beta]-lactoglobulin A and Ribonuclease A. These proteins were chosen because they differ substantially in relative hydrophobicity. The proteins were destabilized by the addition of urea, 4.8 M for [beta]-lactoglobulin A, 6.4 M for Ribonuclease A. At these urea concentrations the proteins are just beginning to unfold. Addition of small amounts of a second denaturant produced changes in the levorotation of the proteins; these changes are used to determine a quantitative estimate of the denaturant's potency. With this procedure, denaturation transitions should approach a two-state mechanism and the product formed should approach a randomly-coiled conformation. |
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