Study by PMR spectroscopy and gel chromatography of the unfolding of substituted kerateines in 8 M urea.
Various S-substituted derivatives of the reduced low sulphur and high proteins from wool have been prepared in which the substituted group is hydrogen, carboxymethyl, carboxethyl, methyl, carbamidomethyl, cyanoethyl and aminoethyl. The proton magnetic resonance (PMR) spectra and gel filtration chromatography of these proteins have been examined in 8 M urea solution as a function of pH in order to determine conditions under which the proteins occur as random coils in solution with no evidence for the occurrence of non-covalent interactions. The PMR method described in an earlier paper (1) provides an easier and much more sensitive method for the observation of non-covalent interactions in random coil proteins than does the measurement of elution volumes in gel chromatography. The results obtained by both methods are consistent and show that the widest range of pH for which unfolding occurs in 8 M urea is obtained with the S-carboxymethyl, S-carboxyethyl, S-methyl and S-carbamidomethyl derivatives.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D007633:Keratins / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D008970:Molecular Weight; D014508:Urea; D014935:Wool / Q000032:analysis*
D000596:Amino Acids; D007633:Keratins; D014508:Urea