期刊
MAGNETIC RESONANCE IN CHEMISTRY
卷 42, 期 2, 页码 162-171出版社
WILEY
DOI: 10.1002/mrc.1320
关键词
NMR; PISEMA; dipolar couplings; micelle; bicelle; bilayer; PISA Wheel; Dipolar Waves; membrane protein
资金
- NIBIB NIH HHS [P41EB001966] Funding Source: Medline
- NIGMS NIH HHS [P01GM64676, R37GM24266, R01GM29754] Funding Source: Medline
The paper briefly reviews the process of determining the structures of membrane proteins by NMR spectroscopy of aligned samples, describes the integration of recent developments in the interpretation of spectra of aligned proteins and illustrates the application of these methods to the trans-membrane helical domain of a protein. The emerging methods of interpreting the spectral parameters from aligned samples of isotopically labeled proteins provide opportunities for simultaneously assigning the spectra and determining the structures of the proteins, and also for comparing the results from solid-state NMR experiments on completely aligned samples with those of solution NMR experiments on weakly aligned samples. Copyright (C) 2004 John Wiley Sons, Ltd.
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