A method is presented for the calculation of REDOR dephasing for specifically labeled membrane-spanning peptides in uniformly aligned lipid bilayers under magic angle oriented sample spinning (MAOSS) conditions. Numerical simulations are performed for dephasing of 13 C signal by 15 N when the labels
NMR of peptides and proteins in oriented membranes
β Scribed by Marassi, Francesca M.
- Publisher
- John Wiley and Sons
- Year
- 2002
- Tongue
- English
- Weight
- 364 KB
- Volume
- 14
- Category
- Article
- ISSN
- 1043-7347
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β¦ Synopsis
Abstract
Solidβstate NMR spectroscopy is used to determine the structures of membrane peptides and proteins in lipid bilayers. The methodology for membrane protein structure determination using solidβstate NMR of oriented lipid bilayer samples is outlined. Recent developments in recombinant bacterial expression systems for the preparation of isotopically labeled membrane proteins, pulse sequences for highβresolution spectroscopy, and structural indices that guide the structure assembly process greatly extend the capabilities of the technique. Β© 2002 Wiley Periodicals, Inc. Concepts in Magn Reson 14, 212β224, 2002.
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The orientations of helical peptides in membrane bilayers provide important structural information that is directly relevant to their functional roles, both alone and within the context of larger membrane proteins. The orientations can be readily determined with solid state NMR experiments on sample
Membrane proteins are a major challenge for structural biology. The membrane adds an important constraint to their structure, which makes it necessary not only to obtain distance but also orientational information. Solid-state NMR on oriented immobile molecular systems provides information for relat