Secondary and tertiary structure formation of the β-barrel membrane protein OmpA is synchronized and depends on membrane thickness

Journal of Molecular Biology

Volumn 324, Issue 2, 2002, Pages 319-330

  Kleinschmidt, Jörg H ^a,b   Tamm, Lukas K ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b UNIVERSITY OF KONSTANZ   (Germany)

Author keywords

Folding kinetics; Membrane protein folding; Outer membrane protein A; Synchronized structure formation; barrel membrane protein

Indexed keywords

DILAURYLPHOSPHATIDYLCHOLINE; MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN A; PHOSPHATIDYLCHOLINE; UNCLASSIFIED DRUG;

ARTICLE; BETA SHEET; CIRCULAR DICHROISM; ESCHERICHIA COLI; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; GEL ELECTROPHORESIS; HYDROGEN BOND; HYDROPHOBICITY; KINETICS; LIPID BILAYER; MEMBRANE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; THICKNESS;

ESCHERICHIA COLI; INSERTION SEQUENCES;

EID: 0036441481     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01071-9     Document Type: Article

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