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Sergeyev IV1, Bahri S1, Day LA2, McDermott AE1.
The Journal of chemical physics.J Chem Phys.2014 Dec 14;141(22):22D533. doi: 10.1063/1.4903230.
High resolution two- and three-dimensional heteronuclear correlation spectroscopy ((1)H-(13)C, (1)H-(15)N, and (1)H-(13)C-(13)C HETCOR) has provided a detailed characterization of the internal and external hydration water of the Pf1 virion. This long and slender virion (2000 nm × 7 nm) contains hig
PMID 25494804

Structure refinement and membrane positioning of selectively labeled OmpX in phospholipid nanodiscs.

Hagn F1, Wagner G.
Journal of biomolecular NMR.J Biomol NMR.2014 Nov 28. [Epub ahead of print]
NMR structural studies on membrane proteins are often complicated by their large size, taking into account the contribution of the membrane mimetic. Therefore, classical resonance assignment approaches often fail. The large size of phospholipid nanodiscs, a detergent-free phospholipid bilayer mimeti
PMID 25430058

Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings.

Bibow S1, Carneiro MG, Sabo TM, Schwiegk C, Becker S, Riek R, Lee D.
Protein science : a publication of the Protein Society.Protein Sci.2014 Jul;23(7):851-6. doi: 10.1002/pro.2482. Epub 2014 May 6.
Membrane proteins are involved in numerous vital biological processes. To understand membrane protein functionality, accurate structural information is required. Usually, structure determination and dynamics of membrane proteins are studied in micelles using either solution state NMR or X-ray crysta
PMID 24752984