%0 Journal Article %1 park_nanodiscs_2011 %A Park, Sang Ho %A Berkamp, Sabrina %A Cook, Gabriel A %A Chan, Michelle K %A Viadiu, Hector %A Opella, Stanley J %D 2011 %J Biochemistry %K Artificial,Bacterial Mimicry,X-Ray Proteins,Bacteriorhodopsins,Crystallography,Lipid Proteins,Membranes,Molecular Resonance Spectroscopy,Membrane bilayers,Magnetic %N 42 %P 8983--8985 %R 10.1021/bi201289c %T Nanodiscs versus macrodiscs for \NMR\ of membrane proteins %V 50 %X It is challenging to find membrane mimics that stabilize the native structures, dynamics, and functions of membrane proteins. In a recent advance, nanodiscs have been shown to provide a bilayer environment compatible with solution NMR. We show that increasing the lipid to "belt" peptide ratio expands their diameter, slows their reorientation rate, and allows the protein-containing discs to be aligned in a magnetic field for oriented sample solid-state NMR. The spectroscopic properties of membrane proteins with one to seven transmembrane helices in q = 0.1 isotropic bicelles, \$\backslash$textasciitilde\10 nm diameter isotropic nanodiscs, \$\backslash$textasciitilde\30 nm diameter magnetically aligned macrodiscs, and q = 5 magnetically aligned bicelles are compared.

@article{park_nanodiscs_2011, abstract = {It is challenging to find membrane mimics that stabilize the native structures, dynamics, and functions of membrane proteins. In a recent advance, nanodiscs have been shown to provide a bilayer environment compatible with solution NMR. We show that increasing the lipid to "belt" peptide ratio expands their diameter, slows their reorientation rate, and allows the protein-containing discs to be aligned in a magnetic field for oriented sample solid-state NMR. The spectroscopic properties of membrane proteins with one to seven transmembrane helices in q = 0.1 isotropic bicelles, {\{}$\backslash$textasciitilde{\}}10 nm diameter isotropic nanodiscs, {\{}$\backslash$textasciitilde{\}}30 nm diameter magnetically aligned macrodiscs, and q = 5 magnetically aligned bicelles are compared.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Park, Sang Ho and Berkamp, Sabrina and Cook, Gabriel A and Chan, Michelle K and Viadiu, Hector and Opella, Stanley J}, biburl = {https://www.bibsonomy.org/bibtex/2594efc6c81f3045dbe8d6ee5f5d172ec/nmrresource}, doi = {10.1021/bi201289c}, interhash = {ecf230ebc74ae2d2b40b9cde33374da0}, intrahash = {594efc6c81f3045dbe8d6ee5f5d172ec}, issn = {1520-4995}, journal = {Biochemistry}, keywords = {Artificial,Bacterial Mimicry,X-Ray Proteins,Bacteriorhodopsins,Crystallography,Lipid Proteins,Membranes,Molecular Resonance Spectroscopy,Membrane bilayers,Magnetic}, month = oct, number = 42, pages = {8983--8985}, pmid = {21936505}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Nanodiscs versus macrodiscs for {\{}NMR{\}} of membrane proteins}}, volume = 50, year = 2011 }