Escherichia coli OmpA retains a folded structure in the presence of sodium dodecyl sulfate due to a high kinetic barrier to unfolding

Biochimica et Biophysica Acta - Biomembranes

Volumn 1515, Issue 2, 2001, Pages 159-166

  Ohnishi, Satoshi ^b   Kameyama, Keiichi ^a  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

Folding kinetics; Membrane protein; OmpA; Protein folding; Stability

Indexed keywords

BACTERIAL PROTEIN; DODECYL SULFATE SODIUM; OCTYL GLUCOSIDE; OUTER MEMBRANE PROTEIN A; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL REACTION; CIRCULAR DICHROISM; DENATURATION; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; HEATING; KINETICS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; TEMPERATURE;

CIRCULAR DICHROISM; ESCHERICHIA COLI; GLUCOSIDES; HEAT; ORGANOPHOSPHORUS COMPOUNDS; PROTEIN FOLDING; SODIUM DODECYL SULFATE; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; SURFACE-ACTIVE AGENTS;

ESCHERICHIA COLI;

EID: 0035575842     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(01)00410-2     Document Type: Article

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