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Abstract Reduced proteins in aqueous solutions of 6 m guanidine hydrochloride or sodium dodecyl sulfate assume conformations such that the hydrodynamic shape varies predictably with molecular weight. Consequently, gel chromatography can be used to determine both effective hydrodynamic radii and molecular weights of polypeptide chains in these solvents. Data obtained with the same support media in the two different solvent systems suggest that gel chromatography can be used as a substitute for other hydrodynamic measurements in the determination of gross conformation of proteins in these solvents.
Fish et al. (Thu,) studied this question.