Helical and expanded conformation of equine β-lactoglobulin in the cold-denatured state

Journal of Molecular Biology

Volumn 350, Issue 2, 2005, Pages 338-348

  Yamada, Yoshiteru ^a   Yajima, Takeo ^a   Fujiwara, Kazuo ^a   Arai, Munehito ^b,e   Ito, Kazuki ^c,f   Shimizu, Akio ^a   Kihara, Hiroshi ^d   Kuwajima, Kunihiro ^b   Amemiya, Yoshiyuki ^b   Ikeguchi, Masamichi ^a  

^a SOKA UNIVERSITY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c UNIVERSITY OF TSUKUBA   (Japan)

^d KANSAI MEDICAL UNIVERSITY   (Japan)

^e NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^f RIKEN HARIMA INSTITUTE   (Japan)

Author keywords

Folding; Molten globule; Sedimentation coefficient; Small angle X ray scattering; Stability

Indexed keywords

BETA LACTOGLOBULIN;

ARTICLE; CIRCULAR DICHROISM; COLD; DENATURATION; HEAT; MOLECULAR SIZE; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; RADIATION SCATTERING; TEMPERATURE; TEMPERATURE DEPENDENCE; ULTRACENTRIFUGATION;

EQUIDAE;

EID: 20444382418     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.003     Document Type: Article

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