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- W2313227002 abstract "We demonstrated here that high-resolution solid-state NMR is a very convenient means to analyze conformation and dynamics of membrane proteins such as bacteriorhodopsin (bR) and their fragments incorporated into bilayers, if an appropriate 13C-labelling is feasible either by biosynthesis or chemical synthesis. We assigned regio-specifically resolved 13C NMR peaks of [3-13C] Ala-bR to the transmembrane helices, N-or C-terminus and loop regions with reference to the conformation-dependent 13C chemical shifts so far accumulated. Further assignment of these signals to individual residues has been made on the basis of a variety of experiments, comparison of spectra between wild type and site-directed mutants, enzymatic digestion, pH changes, etc. This approach turned out to be an excellent means to probe conformational changes induced by lipid-protein interaction, cation-binding, etc. We also demonstrated a novel approach to probe the manner of interaction of biologically active peptides with lipids by utilizing magnetically oriented lipid bilayers or bicelles." @default.
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- W2313227002 date "1998-01-01" @default.
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- W2313227002 title "Conformation and Dynamics of Membrane Proteins as Revealed by High-resolution Solid-state NMR." @default.
- W2313227002 doi "https://doi.org/10.5360/membrane.23.162" @default.
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