The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment

Protein Science

Volumn 14, Issue 4, 2005, Pages 856-861

  Duong Ly, Krisna C ^a   Nanda, Vikas ^b   DeGrado, William F ^b   Howard, Kathleen P ^a  

^a SWARTHMORE COLLEGE   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

EPR spectroscopy; Helix tilt; Hydrophobic mismatch; Lateral pressure; M2 proton channel; Membrane protein structure; Peptide lipid interactions; Site directed spin labeling

Indexed keywords

GLYCEROPHOSPHORYLCHOLINE; ION CHANNEL; LIPID; MEMBRANE PROTEIN; NITROXIDE; PROTEIN; PROTEIN M2; PROTON; TETRAMER;

AMINO TERMINAL SEQUENCE; ARTICLE; ELECTRON SPIN RESONANCE; HYDROPHOBICITY; INFLUENZA VIRUS A; LIPID BILAYER; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE; SPIN LABELING;

ELECTRON SPIN RESONANCE SPECTROSCOPY; ION CHANNELS; LIPID BILAYERS; MODELS, MOLECULAR; PROTEIN CONFORMATION; VIRAL MATRIX PROTEINS;

EID: 15244348542     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041185805     Document Type: Article

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