Abstract
Measurements have been made of the intrinsic viscosities of proteins consisting of one polypeptide chain, in 6 M guanidine hydrochloride plus 0-mercaptoethanol at different temperatures in the range 25-55'. The molecular weight de- pendence and the values of Huggins constant and end-to-end distance were determined at 25 for the reduced denatured proteins including papain and were consistent with their linear random coil behavior. The behavior of reduced ovalbumin in 9 M urea was found to be similar. The dimensions of randomly coiled proteins generally decreased with increasing tempera- ture. The unperturbed dimensions calculated from viscosity I ntrinsic viscosity measurements have been successfully used in the detection of conformational changes in proteins
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