Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.
It is demonstrated here how the secondary structure and dynamics of transmembrane helices, as well as surface residues, such as interhelical loops and N- or C-terminus of bacteriorhodopsin (bR) in purple membrane, can be determined at ambient temperature based on very simple (13)C-NMR measurements, together with a brief experimental background. In contrast to the static picture of bR, currently available from X-ray diffraction or cryo-electron microscopy, the structure consists of dynamically heterogeneous domains which undergo various types of local fluctuations with a frequency range of 10(2)--10 (8) Hz. The significance of this picture is discussed in relation to the biological function of this protein.
Saitô
H
H
Department of Life Science, Faculty of Science, Himeji Institute of Technology, Harima Science Garden City, Kouto 3-chome, Kamigori, 678-1297, Hyogo, Japan. saito@sci.himeji-tech.ac.jp
Tuzi
S
S
Yamaguchi
S
S
Tanio
M
M
Naito
A
A
D001436:Bacteriorhodopsins / Q000737:chemistry*; D002247:Carbon Isotopes; D009682:Magnetic Resonance Spectroscopy; D009038:Motion; D011487:Protein Conformation; D017494:Proton Pumps
D002247:Carbon Isotopes; D017494:Proton Pumps; D001436:Bacteriorhodopsins; C017827:bacterio-opsin