Protein dissection enhances the amyloidogenic properties of α-lactalbumin

FEBS Journal

Volumn 272, Issue 9, 2005, Pages 2176-2188

  De Laureto, Patrizia Polverino ^a   Frare, Erica ^a   Battaglia, Francesca ^a   Mossuto, Maria F ^a   Uversky, Vladimir N ^b,c,d   Fontana, Angelo ^a  

^a UNIVERSITY OF PADOVA   (Italy)

^b INSTITUTE FOR BIOLOGICAL INSTRUMENTATION   (Russian Federation)

^c INDIANA UNIVERSITY   (United States)

^d Molecular Kinetics Inc   (United States)

Author keywords

lactalbumin; Amyloid; Circular dichroism; Infrared spectroscopy; Limited proteolysis; Molten globule; Protein aggregation

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALPHA LACTALBUMIN; AMYLOID; AMYLOID BETA PROTEIN;

ACIDITY; AMINO ACID SEQUENCE; AMYLOIDOSIS; ARTICLE; CHEMICAL BOND; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; HYDROPHOBICITY; INFRARED SPECTROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN HYDROLYSIS; REACTION ANALYSIS;

AMINO ACID SEQUENCE; AMYLOID; ANIMALS; CATTLE; CIRCULAR DICHROISM; HUMANS; HYDROGEN; HYDROGEN-ION CONCENTRATION; LACTALBUMIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SWINE;

EID: 18444375570     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04638.x     Document Type: Article

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