Juxtamembrane tryptophans have distinct roles in defining the OmpX barrel-micelle boundary and facilitating protein-micelle association

FEBS Letters

Volumn 588, Issue 23, 2014, Pages 4464-4471

  Chaturvedi, Deepti ^a   Mahalakshmi, Radhakrishnan ^a  

^a Transit Campus: ITI   (India)

Author keywords

Beta barrel folding; Fluorescence anisotropy; Fluorescence lifetime; Membrane protein biophysics; Protein micelle interface; Tryptophan detergent interaction

Indexed keywords

OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN X; TRYPTOPHAN; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; HYDROLASE; MICELLE; OMPX PROTEIN, E COLI; PHOSPHORYLCHOLINE; PROTEIN BINDING; SOLVENT;

ARTICLE; CONTROLLED STUDY; MICELLE; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN REFOLDING; PROTEIN STABILITY; SOLVATION; STRUCTURE ANALYSIS; THERMODYNAMICS; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; METABOLISM; PROTEIN SECONDARY STRUCTURE; TEMPERATURE;

BACTERIAL OUTER MEMBRANE PROTEINS; CELL MEMBRANE; ESCHERICHIA COLI PROTEINS; HYDROLASES; KINETICS; MICELLES; MODELS, MOLECULAR; PHOSPHORYLCHOLINE; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; TEMPERATURE; TRYPTOPHAN;

EID: 84910596744     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.10.017     Document Type: Article

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