Characterization of the mobility of various chemical groups in the purple membrane of halobacterium halobium by 13C, 31P and 2H solid state N M R |
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Authors: | K-H Spohn R Kimmich |
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Institution: | Sektion Kernresonanzspektroskopie Universität Ulm 7900 Ulm, Fed. Rep. Germany |
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Abstract: | Lyophilized purple membrane sheets have been investigated by C-13- and P-31-cross polarization/magic angle spinning N M R spectroscopy. The high-resolution C-13 spectrum and its non-quaternary suppression version indicate fast protein side-chain motions but a rigid backbone structure on a time scale of roughly < 0.001 to 0.01 s. Three components of exchangeable hydrogen have been detected by deuterium N M R. The mean exchange time of the peptide hydrogens must be longer than 1 μs. The medium component is attributed to mobile side-chains. In addition a narrow line has been observed which is assigned to the residual hydration water. |
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