The binding of 3,6-disubstituted bile salts to human serum albumin induces conformational change on the molecule of this protein

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1429, Issue 2, 1999, Pages 299-306

  Farruggia, Beatriz ^a   Picó, Guillermo A ^a  

^a UNIVERSIDAD NACIONAL DE ROSARIO   (Argentina)

Author keywords

Albumin; Bile salt; Calorimetry; Circular dichroism; Tryptophan quenching

Indexed keywords

BILE ACID; HUMAN SERUM ALBUMIN;

ARTICLE; BINDING SITE; CIRCULAR DICHROISM; COMPLEX FORMATION; DIFFERENTIAL SCANNING CALORIMETRY; FLUORESCENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN;

ANILINO NAPHTHALENESULFONATES; BILE ACIDS AND SALTS; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; ENERGY TRANSFER; FLUORESCENT DYES; HUMANS; PROTEIN BINDING; PROTEIN CONFORMATION; SERUM ALBUMIN; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TRYPTOPHAN;

EID: 0032951698     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00192-7     Document Type: Article

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