Dynamic Nuclear Polarization-Enhanced Solid-State NMR of a 13C-Labeled Signal Peptide Bound to Lipid-Reconstituted Sec Translocon
Dynamic Nuclear Polarization-Enhanced Solid-State NMR of a 13C-Labeled Signal Peptide Bound to Lipid-Reconstituted Sec Translocon
Lenica Reggie, Jakob J. Lopez, Ian Collinson, Clemens Glaubitz and Mark Lorch
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja209378h/aop/images/medium/ja-2011-09378h_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja209378h
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1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques.
Related Articles 1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques.
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