Structure determination of aligned samples of membrane proteins by NMR spectroscopy | Zendy

Nevzorov Alexander A. | Zendy; Mesleh Michael F. | Zendy; Opella Stanley J. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

Structure determination of aligned samples of membrane proteins by NMR spectroscopy

Author(s) -

Nevzorov Alexander A.,

Mesleh Michael F.,

Opella Stanley J.

Publication year - 2004

Publication title -

magnetic resonance in chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.483

H-Index - 72

eISSN - 1097-458X

pISSN - 0749-1581

DOI - 10.1002/mrc.1320

Subject(s) - chemistry , nuclear magnetic resonance spectroscopy , spectroscopy , membrane protein , nmr spectra database , analytical chemistry (journal) , membrane , solid state nuclear magnetic resonance , crystallography , spectral line , nuclear magnetic resonance , chromatography , stereochemistry , biochemistry , physics , quantum mechanics , astronomy

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 © 2004 John Wiley & Sons, Ltd.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research