pH-dependent stability of the human α-lactalbumin molten globule state: Contrasting roles of the 6 - 120 disulfide and the β-subdomain at low and neutral pH

Proteins: Structure, Function and Genetics

Volumn 52, Issue 2, 2003, Pages 193-202

  Horng, Jia Cherng ^a   Demarest, Stephen J ^a,b   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b DIVERSA CORPORATION   (United States)

Author keywords

lactalbumin; Molten globule state; pH effects; Protein folding; Protein stability

Indexed keywords

ALPHA LACTALBUMIN; CALCIUM ION; DISULFIDE;

ARTICLE; DISULFIDE BOND; DNA HELIX; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE;

CIRCULAR DICHROISM; DISULFIDES; HUMANS; HYDROGEN-ION CONCENTRATION; LACTALBUMIN; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 0037661368     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10406     Document Type: Article

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