Signal assignment and secondary structure analysis of a uniformly [13C, 15N]-labeled membrane protein, H+-ATP synthase subunit c, by magic-angle spinning solid-state NMR-Reference-Cited by-同舟云学术

Signal assignment and secondary structure analysis of a uniformly [13C, 15N]-labeled membrane protein, H+-ATP synthase subunit c, by magic-angle spinning solid-state NMR

Published:2006-11-02 Issue:4 Volume:36 Page:279-293
ISSN:0925-2738
Container-title:Journal of Biomolecular NMR
language:en
Short-container-title:J Biomol NMR

Author:

Kobayashi Masatoshi,Matsuki Yoh,Yumen Ikuko,Fujiwara Toshimichi,Akutsu Hideo

Publisher

Springer Science and Business Media LLC

Subject

Spectroscopy,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s10858-006-9094-x.pdf

Reference42 articles.

1. Baldus M., Petkova A.T., Herzfeld J., Griffin R.G. (1998). Mol. Phys. 95:1197–1207

2. Bennett A.E., Rienstra C.M., Auger M., Lakshmi K.V., Griffin R.G. (1995). J. Chem. Phys. 103:6951–6958

3. Bennett A.E., Rienstra C.M., Griffiths J.M., Zhen W.G., Lansbury P.T., Griffin R.G. (1998). J. Chem. Phys. 108:9463–9479

4. Böckmann A., Lange A., Galinier A., Luca S., Giraud N., Juy M., Heise H., Montserret R., Penin F., Baldus M. (2003). J. Biomol. NMR 27:323–339

5. Castellani F., van Rossum B., Diehl A., Schubert M., Rehbein K., Oschkinat H. (2002). Nature 420:98–102

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