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.
%0 Journal Article
%1 nevzorov_structure_2004
%A Nevzorov, Alexander A
%A Mesleh, Michael F
%A Opella, Stanley J
%D 2004
%J Magn Reson Chem
%K Acid Acid,Amino Amino Conformation,Protein Fragments,Peptides,Protein Frames,Peptide Homology Proteins,Open Reading Resonance Results,Secondary,Sequence Sequence,Magnetic Spectroscopy,Membrane Structure,Reproducibility of
%N 2
%P 162--171
%R 10.1002/mrc.1320
%T Structure determination of aligned samples of membrane proteins by \NMR\ spectroscopy
%V 42
%X 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.
@article{nevzorov_structure_2004,
abstract = {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.},
added-at = {2017-03-14T02:48:56.000+0100},
author = {Nevzorov, Alexander A and Mesleh, Michael F and Opella, Stanley J},
biburl = {https://www.bibsonomy.org/bibtex/204d87496e59e1a6686ff7c1735ef9a0f/nmrresource},
doi = {10.1002/mrc.1320},
interhash = {c5aaf451b70b9c018d527e281be20992},
intrahash = {04d87496e59e1a6686ff7c1735ef9a0f},
issn = {0749-1581},
journal = {Magn Reson Chem},
keywords = {Acid Acid,Amino Amino Conformation,Protein Fragments,Peptides,Protein Frames,Peptide Homology Proteins,Open Reading Resonance Results,Secondary,Sequence Sequence,Magnetic Spectroscopy,Membrane Structure,Reproducibility of},
month = feb,
number = 2,
pages = {162--171},
pmid = {14745796},
timestamp = {2017-03-14T02:49:21.000+0100},
title = {{Structure determination of aligned samples of membrane proteins by {\{}NMR{\}} spectroscopy}},
volume = 42,
year = 2004
}