CHAPTER 16: Dynamic Structure Analysis of Peptides in Membranes by Solid-State NMR
Published:24 Feb 2014
E. Strandberg and A. S. Ulrich, 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. 304-319.
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Solid-state NMR is the method of choice to determine the structure and mobility of membrane-bound peptides under quasi-native conditions. Information about the orientation of a molecule and its dynamics, however, is intermingled in the measured NMR parameters. Therefore, it is crucial to be able to extract and interpret correctly both types of information to obtain a reliable picture of the peptide and its interactions with the lipid bilayer. In this review we describe a general approach for determining peptide orientations in conjunction with different models that take the peptide dynamics into account. We also discuss problems that can arise from the use of too simplistic models in the case of highly dynamic peptides. These dynamical considerations have turned out to be important, e.g. in studies of the mismatch dependent tilt of transmembrane model peptides, and for very short amphipathic antimicrobial peptides.