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Volumn 383, Issue 2, 2000, Pages 215-224

Thermal cycling aids folding of a recombinant human β-casein with four extra n-terminal amino acid residues

a LOMA LINDA UNIVERSITY SCHOOL OF MEDICINE (United States)

Author keywords

Analytical ultracentrifugation; Circular dichroism; Fluorescence spectroscopy; Human casein; Laser light scattering; Protein folding; Thermal cycling; Turbidity

Indexed keywords

BETA CASEIN; CALCIUM;

AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; LIGHT SCATTERING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE; TEMPERATURE SENSITIVITY; TURBIDITY; ULTRACENTRIFUGATION;

EID: 0034669361 PISSN: 00039861 EISSN: None Source Type: Journal
DOI: 10.1006/abbi.2000.2063 Document Type: Article

Times cited : (6)

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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.