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Solid-state NMR (ssNMR) is a versatile technique that can provide high-resolution (sub-angstrom) structural data for integral membrane proteins embedded in native and model membrane environments. The methodologies for a priori structure determination have for the most part been developed using samples with crystalline and fibrous morphologies. However, the techniques are now being applied to large, polytopic membrane proteins including receptors, ion channels, and porins. ssNMR data may be used to annotate and refine existing structures in regions of the protein not fully resolved by crystallography (including ligand-binding sites and mobile solvent accessible loop regions). This review describes the spectroscopic experiments and data analysis methods (including assignment) used to generate high-resolution structural data for membrane proteins. We also consider the range of sample morphologies that are appropriate for study by this method.

Original publication

DOI

10.1007/978-1-4939-2230-7_17

Type

Journal article

Journal

Methods Mol Biol

Publication Date

2015

Volume

1261

Pages

331 - 347

Keywords

Binding Sites, Membrane Proteins, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation