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pubmed-article:10984589pubmed:abstractTextIt 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.lld:pubmed
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pubmed-article:10984589pubmed:articleTitleConformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.lld:pubmed
pubmed-article:10984589pubmed:affiliationDepartment 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.jplld:pubmed
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