CHAPTER 18: Helical Membrane Protein Structure: Strategy for Success
Published:24 Feb 2014
N. Das, D. T. Murray, Y. Miao, and T. A. Cross, 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. 353-370.
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Solid-state NMR provides a unique technology for the characterization of membrane proteins in liquid crystalline lipid bilayer preparations. Since protein structure is the result of interactions within the protein and between the protein and its environment, it is important to model the native environment as accurately as possible. Helical membrane protein structures have a fragile tertiary and quaternary structure that is particularly sensitive to these environmental influences. The combination of orientational restraints obtained from oriented sample solid-state NMR and distance restraints obtained from magic angle spinning NMR provide an excellent strategy for the characterization of membrane proteins.