Molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: A comparative analysis by circular dichroism spectroscopy and limited proteolysis

Proteins: Structure, Function and Genetics

Volumn 49, Issue 3, 2002, Pages 385-397

  De Laureto, Patrizia Polverino ^a   Frare, Erica ^a   Gottardo, Rossella ^a   Fontana, Angelo ^a  

^a UNIVERSITY OF PADOVA   (Italy)

Author keywords

lactalbumin; Circular dichroism; HAMLET; Limited proteolysis; Molten globule; Protein folding; Protein fragments; Trifluoroethanol

Indexed keywords

ALPHA LACTALBUMIN; OLEIC ACID; PROTEIN; PROTEIN HAMLET; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; APOPTOSIS; AQUEOUS SOLUTION; ARTICLE; CATTLE; CIRCULAR DICHROISM; COMPARATIVE STUDY; HEATING; NONHUMAN; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INDUCTION; PROTEIN VARIANT; ROOM TEMPERATURE; TEMPERATURE DEPENDENCE; TUMOR CELL;

ANIMALS; APOPROTEINS; CATTLE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPEPTIDASE K; HEAT; HYDROGEN-ION CONCENTRATION; LACTALBUMIN; MODELS, CHEMICAL; OLEIC ACID; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; TRIFLUOROETHANOL;

BOVINAE;

EID: 0037110569     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10234     Document Type: Article

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