FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein.
Nazarov, Petr V
FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein. [electronic resource] - Biophysical journal Feb 2007 - 1296-305 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-3495
10.1529/biophysj.106.095026 doi
Bacteriophage M13--chemistry
Capsid Proteins--chemistry
Computer Simulation
Cysteine--chemistry
Fluorescence Resonance Energy Transfer
Fluorescent Dyes
Lipid Bilayers--chemistry
Membrane Proteins--chemistry
Models, Biological
Mutagenesis, Site-Directed
Naphthalenesulfonates
Phosphatidylcholines--chemistry
Phosphatidylglycerols--chemistry
Protein Structure, Tertiary
FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein. [electronic resource] - Biophysical journal Feb 2007 - 1296-305 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-3495
10.1529/biophysj.106.095026 doi
Bacteriophage M13--chemistry
Capsid Proteins--chemistry
Computer Simulation
Cysteine--chemistry
Fluorescence Resonance Energy Transfer
Fluorescent Dyes
Lipid Bilayers--chemistry
Membrane Proteins--chemistry
Models, Biological
Mutagenesis, Site-Directed
Naphthalenesulfonates
Phosphatidylcholines--chemistry
Phosphatidylglycerols--chemistry
Protein Structure, Tertiary