Amphipol-Trapped ExbB–ExbD Membrane Protein Complex from Escherichia coli: A Biochemical and Structural Case Study

Journal of Membrane Biology

Volumn 247, Issue 9-10, 2014, Pages 1005-1018

  Sverzhinsky, Aleksandr ^a   Qian, Shuo ^b   Yang, Lin ^c   Allaire, Marc ^c   Moraes, Isabel ^d,e,f   Ma, Dewang ^g   Chung, Jacqueline W ^a   Zoonens, Manuela ^h,i   Popot, Jean Luc ^h,i   Coulton, James W ^a,j  

^a MCGILL UNIVERSITY   (Canada)

^b OAK RIDGE NATIONAL LABORATORY   (United States)

^c BROOKHAVEN NATIONAL LABORATORY   (United States)

^d DIAMOND LIGHT SOURCE LTD   (United Kingdom)

^e RUTHERFORD APPLETON LABORATORY   (United Kingdom)

^f IMPERIAL COLLEGE LONDON   (United Kingdom)

^g UNIVERSITÉ DE MONTRÉAL   (Canada)

^h INST DE BIOLOGIE PHYSICO CHIMIQUE   (France)

ⁱ UNIVERSITÉ PARIS DESCARTES   (France)

^j Microbiome and Disease Tolerance Centre   (Canada)

more..

Author keywords

Amphipol; Detergent; EM; Membrane protein complex; SAXS SANS

Indexed keywords

AMPHIPOL; BACTERIAL PROTEIN; EXBB PROTEIN; EXBD PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; AMPHIPOL A8-35; ESCHERICHIA COLI PROTEIN; EXBB PROTEIN, E COLI; EXBD PROTEIN, E COLI; MULTIPROTEIN COMPLEX; OUTER MEMBRANE PROTEIN; POLYMER; PROPYLAMINE; PROTEIN BINDING; SURFACTANT;

ARTICLE; ELECTRON MICROSCOPY; ESCHERICHIA COLI; FIELD FLOW FRACTIONATION; GEL ELECTROPHORESIS; GEL PERMEATION CHROMATOGRAPHY; NEUTRON SCATTERING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN STRUCTURE; QUANTITATIVE ASSAY; THERMOSTABILITY; ULTRACENTRIFUGATION; X RAY CRYSTALLOGRAPHY; BINDING SITE; CHEMICAL PHENOMENA; CHEMISTRY; PROTEIN CONFORMATION; SOLUBILITY; ULTRASTRUCTURE;

BACTERIAL OUTER MEMBRANE PROTEINS; BINDING SITES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MULTIPROTEIN COMPLEXES; POLYMERS; PROPYLAMINES; PROTEIN BINDING; PROTEIN CONFORMATION; SOLUBILITY; SURFACE-ACTIVE AGENTS;

EID: 84911003599     PISSN: 00222631     EISSN: 14321424     Source Type: Journal    
DOI: 10.1007/s00232-014-9678-4     Document Type: Article

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