A comparative study of the α-subdomains of bovine and human α-lactalbumin reveals key differences that correlate with molten globule stability

Protein Science

Volumn 14, Issue 1, 2005, Pages 89-96

  Chowdhury, Farhana A ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

lactalbumin; A state; Molten globule; Partially folded states; Protein folding; Protein stability

Indexed keywords

ALPHA LACTALBUMIN; GLOBULIN;

ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPARATIVE STUDY; COW; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ANIMALS; CATTLE; HUMANS; LACTALBUMIN; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; UREA;

BOVINAE;

EID: 11144235692     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04977905     Document Type: Article

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