Journal
MAGNETIC RESONANCE IN CHEMISTRY
Volume 42, Issue 2, Pages 162-171Publisher
WILEY
DOI: 10.1002/mrc.1320
Keywords
NMR; PISEMA; dipolar couplings; micelle; bicelle; bilayer; PISA Wheel; Dipolar Waves; membrane protein
Funding
- NIBIB NIH HHS [P41EB001966] Funding Source: Medline
- NIGMS NIH HHS [P01GM64676, R37GM24266, R01GM29754] Funding Source: Medline
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available