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Nanodiscs versus macrodiscs for NMR of membrane proteins.

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, ~10 nm diameter isotropic nanodiscs, ~30 nm diameter magnetically aligned macrodiscs, and q = 5 magnetically aligned bicelles are compared.

SUBMITTER: Park SH

PROVIDER: S-EPMC3236031 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

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Nanodiscs versus macrodiscs for NMR of membrane proteins.

Park Sang Ho SH Berkamp Sabrina S Cook Gabriel A GA Chan Michelle K MK Viadiu Hector H Opella Stanley J SJ

Biochemistry 20110930 42

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 membran ...[more]

PMID: 21936505

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