Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, α-Chymotrypsin, and b-Lactoglobulin

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Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, &Zhymotrypsin, and @Lactoglobulin*

The unfolding of ribonuclease, lysozyme, a-chymotrypsin, and goat P-lactoglobulin by urea and guanidine hydrochloride (GmHCl) has been followed with the use of optical rotation measurements. Urea denaturation leads to a more negative rotation for each protein than does GmHCl denaturation, but the concentration dependence is such that the rotations are almost identical in the absence of denatura...

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Estimation of the free energy of stabilization of ribonuclease A, lysozyme, alpha-lactalbumin, and myoglobin.

The denaturation of ribonuclease A, lysozyme alpha-lactalbumin, and myoglobin by urea, guanidine hydrochloride, and guanidine thiocyanate has been followed with the use of difference spectral measurements. The free energy of stabilization (delta GH2OD) has been determined by the linear extrapolation of the free energy of denaturation to zero denaturant concentration. The values of delta GH2OD a...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1974

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(20)79739-5