Effects of sodium dodecyl sulfate, guanidine hydrochloride, urea, and heat on denaturation of sulfur rich protein in soybeans (Glycine max L.)
2001
Sze-Tao, K.W.C. | Sathe, S.K.
Soybean sulfur-rich protein (SRP) has a stable hydrophobic interior that is resistant to denaturation and unfolding. About half of the tryptophan residues in native SRP are inaccessible to acrylamide quenching. Maximum unfolding, as assessed by fluorescence quenching experiments, was afforded by 2 M urea, 6 M guanidine HCl and 30 min moist heat. Sodium dodecyl sulfate (SDS) did not improve tryptophan accessibility to acrylamide quenching. SRP tryptophan residues were minimally accessible to the iodide quenching indicating a nonionic environment around the majority of the tryptophan residues in SRP.
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