Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties

Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 31, 2006, Pages 11509-11514

  Boldog, Thomas ^a,c   Grimme, Stephen ^b   Li, Mingshan ^a   Sligar, Stephen G ^b   Hazelbauer, Gerald L ^a  

^a University of Missouri   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^c BOEHRINGER INGELHEIM RCV GMBH AND CO KG   (Austria)

Author keywords

Membrane protein; Nanoparticle; Self assembly; Transmembrane receptor; Transmembrane signaling

Indexed keywords

DIMER; HOMODIMER; MEMBRANE PROTEIN; MEMBRANE RECEPTOR; NANOPARTICLE; OLIGOMER; PHOSPHOTRANSFERASE; PROTEIN HISTIDINE KINASE;

ADAPTATION; ARTICLE; BACTERIUM; CHEMORECEPTOR; CHEMOTAXIS; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME STRUCTURE; LIGAND BINDING; LIPID BILAYER; MOLECULAR INTERACTION; NANODISC; NANOTECHNOLOGY; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN INTERACTION; SIGNAL TRANSDUCTION;

DIMERIZATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; LIPID BILAYERS; MEMBRANE PROTEINS; MODELS, MOLECULAR; NANOTECHNOLOGY; PROTEIN STRUCTURE, QUATERNARY; SIGNAL TRANSDUCTION;

BACTERIA (MICROORGANISMS);

EID: 33746856934     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0604988103     Document Type: Article

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