Differences between the pressure- and temperature-induced denaturation and aggregation of β-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering

Biochemistry

Volumn 38, Issue 20, 1999, Pages 6512-6519

  Panick, Gunda ^a   Malessa, Ralf ^a   Winter, Roland ^a  

^a TU DORTMUND UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTOGLOBULIN;

ARTICLE; DENATURATION; GENETIC VARIABILITY; HYDROPHOBICITY; INFRARED SPECTROSCOPY; PRESSURE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; RADIATION SCATTERING; X RAY DIFFRACTION;

AMINO ACID SUBSTITUTION; ANIMALS; CATTLE; LACTOGLOBULINS; PRESSURE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SCATTERING, RADIATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; X-RAYS;

EID: 0033580649     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982825f     Document Type: Article

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