Description: Integral membrane proteins in nanodiscs can be studied by solution NMR spectroscopy

This title appears in the Scientific Report : 2009

Integral membrane proteins in nanodiscs can be studied by solution NMR spectroscopy

We present a two-dimensional solution NMR spectrum of an integral membrane protein (IMP) in a nanodisc. Solution NMR relies on rapid isotropic tumbling of the analyte with correlation times in the nanosecond range. IMPs in a cellular membrane do not satisfy this condition. Previous liquid-state NMR...

Personal Name(s):	Glück, J.M.
	Wittlich, M. / Feuerstein, S.E. / Hoffmann, S. / Willbold, D. / Koenig, B. W.
Contributing Institute:	Strukturbiochemie; ISB-3 JARA - HPC; JARA-HPC
Published in:	Journal of the American Chemical Society, 131 (2009) S. 12060 - 12061
Imprint:	Washington, DC American Chemical Society 2009
Physical Description:	12060 - 12061
DOI:	10.1021/ja904897p
PubMed ID:	19663495
Document Type:	Journal Article
Research Program:	Funktion und Dysfunktion des Nervensystems
Series Title:	Journal of the American Chemical Society 131
Subject (ZB):	Antigens, CD4: chemistry Antigens, CD4: genetics Humans Magnetic Resonance Spectroscopy Membrane Proteins: chemistry Membrane Proteins: genetics Membranes, Artificial Nanostructures: chemistry Solutions Antigens, CD4 Membrane Proteins J
	Publikationsportal JuSER

Please use the identifier: http://dx.doi.org/10.1021/ja904897p in citations.

We present a two-dimensional solution NMR spectrum of an integral membrane protein (IMP) in a nanodisc. Solution NMR relies on rapid isotropic tumbling of the analyte with correlation times in the nanosecond range. IMPs in a cellular membrane do not satisfy this condition. Previous liquid-state NMR studies on IMPs were conducted in organic solvent or artificial membrane mimicking particles like detergent micelles. Nanodiscs are relatively small (150 kDa), detergent-free model membranes that are suitable for functional reconstitution of IMPs. Nanodiscs allow solubilization of integral membrane proteins in a nearly native lipid bilayer environment. The 70 residue polypeptide CD4mut was incorporated into nanodiscs. CD4mut features one transmembrane helix. The aliphatic (1)H-(13)C HSQC spectrum of nanodiscs with inserted, ((13)C, (15)N)-labeled CD4mut exhibits reasonably dispersed protein and lipid NMR signals. Our results demonstrate that IMPs in nanodiscs are amenable to liquid-state NMR methodology.