Abstract
It is challenging to find membrane mimics that stabilize the native structure, dynamics, and functions of membrane proteins. In a recent advance, nanodiscs have been shown to provide a bilayer environment compatible with solution NMR. Increasing the lipid to "belt" peptide ratio expands their diameter, slows their reorientation rate, and enables the protein-containing discs to be aligned in a magnetic field for Oriented Sample solid-state NMR. Here, we compare the spectroscopic properties of membrane proteins with between one and seven trans-membrane helices in q=0.1 isotropic bicelles, ~10 nm diameter isotropic nanodiscs, ~30 nm diameter magnetically aligned macrodiscs, and q=5 bicelles.
PMID: 21936505 [PubMed - as supplied by publisher]
Nanodiscs versus Macrodiscs for NMR of Membrane Proteins
Nanodiscs versus Macrodiscs for NMR of Membrane Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi201289c/aop/images/medium/bi-2011-01289c_0002.gif
Biochemistry
DOI: 10.1021/bi201289c
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nmrlearner
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09-30-2011 08:01 PM
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nmrlearner
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Postdoc Membrane Proteins
Postdoc Membrane Proteins
Structural studies of membrane proteins by NMR
A post-doctoral position is available to work on the structural studies of a variety of
membrane proteins (cytochrome P450, cytochrome b5, cytochrome-P450-reductase,
and a combination of these proteins to probe protein-protein interactions)
and amyloid proteins using NMR spectroscopy. We are presently utilizing a combination
of high-resolution solution NMR and solid-state (static and MAS) NMR techniques to
solve high-resolution structures and characterize the dynamics of membrane proteins
embedded in suitable...
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01-12-2011 01:45 PM
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