Title : Local and global cooperativity in the human alpha-lactalbumin molten globule.

Pub. Date : 2004 Apr 16

PMID : 15050830






3 Functional Relationships(s)
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1 NMR spectroscopy has been used to follow the urea-induced unfolding of the low pH molten globule states of a single-disulfide variant of human alpha-lactalbumin ([28-111] alpha-LA) and of two mutants, each with a single proline substitution in a helix. Urea lactalbumin alpha Homo sapiens
2 NMR spectroscopy has been used to follow the urea-induced unfolding of the low pH molten globule states of a single-disulfide variant of human alpha-lactalbumin ([28-111] alpha-LA) and of two mutants, each with a single proline substitution in a helix. Urea lactalbumin alpha Homo sapiens
3 The urea-induced unfolding behavior of [28-111] alpha-LA is similar to that of the four-disulfide form of the protein, except that [28-111] alpha-LA is less stable and has greater cooperativity in the loss of different elements of structure. Urea lactalbumin alpha Homo sapiens