Title : Conformational stability of alpha-lactalbumin missing a peptide bond between Asp66 and Pro67.

Pub. Date : 1994 May

PMID : 7986345






2 Functional Relationships(s)
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1 Secondary structural changes of the cleaved alpha-lactalbumin, in which the two separated polypeptides were joined by disulfide bridges, were examined in solutions of sodium dodecyl sulfate (SDS), urea, and guanidine hydrochloride. Urea lactalbumin alpha Homo sapiens
2 On the other hand, the helical structures of the cleaved alpha-lactalbumin began to be disrupted at low concentrations of guanidine hydrochloride and urea compared with that of the intact protein. Urea lactalbumin alpha Homo sapiens