Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine β-lactoglobulin

Proteins: Structure, Function and Genetics

Volumn 63, Issue 3, 2006, Pages 595-602

  Yamada, Yoshiteru ^a   Nakagawa, Kanako ^a   Yajima, Takeo ^a   Saito, Keiko ^a   Tokushima, Akihito ^a   Fujiwara, Kazuo ^a   Ikeguchi, Masamichi ^a  

^a SOKA UNIVERSITY   (Japan)

Author keywords

lactoglobulin; Disulfide mutant; Thermodynamic consequences

Indexed keywords

ALANINE; BETA LACTOGLOBULIN; CYSTEINE; DISULFIDE; LIPOCALIN; MUTANT PROTEIN; UREA;

ACIDITY; ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; DISSOCIATION; DISULFIDE BOND; HORSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BLOOD LEVEL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; STRUCTURE ANALYSIS; THERMODYNAMICS;

ANIMALS; CONSERVED SEQUENCE; DISULFIDES; HORSES; LACTOGLOBULINS; MUTATION; PROTEIN DENATURATION; THERMODYNAMICS;

EQUIDAE; EQUUS CABALLUS;

EID: 33646054876     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20905     Document Type: Article

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