Significance of low-frequency local fluctuation motions in the transmembrane B and C α-helices of bacteriorhodopsin, to facilitate efficient proton uptake from the cytoplasmic surface, as revealed by site-directed solid-state 13C NMR

European Biophysics Journal

Volumn 33, Issue 7, 2004, Pages 580-588

  Kira, Atsushi ^a   Tanio, Michikazu ^a   Tuzi, Satoru ^a   Saitô, Hazime ^a  

^a UNIVERSITY OF HYOGO   (Japan)

Author keywords

Bacteriorhodopsin; Conformation and dynamics change; Low frequency local fluctuations; Proton uptake; Site directed solid state 13C NMR

Indexed keywords

ASPARTIC ACID; BACTERIORHODOPSIN; CARBON 13; PROLINE; PROTON; SCHIFF BASE; VALINE;

ALPHA HELIX; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CONFORMATION; CONTROLLED STUDY; CYTOPLASM; DYNAMICS; ENVIRONMENT; HYDROPHILICITY; HYDROPHOBICITY; ISOTOPE LABELING; MECHANICS; MEMBRANE; MEMBRANE POTENTIAL; MUTANT; NONHUMAN; PH; PROTON TRANSPORT; RECORDING; SOLID STATE; SURFACE PROPERTY;

BACTERIORHODOPSINS; CARBON ISOTOPES; CELL MEMBRANE; CYTOPLASM; LIGHT; LINEAR ENERGY TRANSFER; MAGNETIC RESONANCE SPECTROSCOPY; MOTION; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTON PUMPS; PROTONS; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 11144271469     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-004-0406-3     Document Type: Article

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