CHAPTER 12: Investigations of the Structure, Topology and Dynamics of Membrane-Associated Polypeptides by Solid-State NMR Spectroscopy
Published:24 Feb 2014
E. S. Salnikov, C. Aisenbrey, J. Raya, and B. Bechinger, in Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides, ed. F. Separovic and A. Naito, The Royal Society of Chemistry, 2014, pp. 214-234.
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Solid-state NMR spectroscopy is a unique tool to investigate membrane-associated peptides and proteins in liquid disordered lipid bilayers at atomic resolution. This review provides an overview of magic angle spinning and oriented solid-state NMR spectroscopic investigations of various polypeptides, as well as membrane systems that have been used for such investigations. A focus of the paper is on oriented solid-state NMR, which uses planar supported lipid bilayers or bicelles that align in the magnetic field of the spectrometer. After presenting some theoretical background, the strategy of how to extract structural information from oriented membrane samples is illustrated using spectra from a transmembrane model peptide. Furthermore, the potential sources of experimental and systematic errors and the consequences these have on the accuracy of the resulting structures are discussed.