• Journal of Photoscience
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• v.9 no.2
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• pp.110-113
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• 2002

We demonstrate here a dynamic structure of bacteriorhodopsin (bR) as revealed by $^{13}$ C NMR studies on [3_$^{13}$ C]_,[1-$^{13}$ C]Ala- and/or Val-labeled wild type and a variety of site-directed mutants at ambient temperature. For this purpose, well-resolved (up to twelve) I$^{13}$ C NMR peaks were assigned with reference to the displacement of peaks due to the conformation-dependent I$^{13}$ C chemical shifts and reduced peak-intensities due to site-directed mutations. Revealed bR structure was not rigid as anticipated from 2D crystals of hexagonal array but a dynamically heterogeneous, undergoing a variety of local fluctuations depending upon specific site with frequency range of 10$^2$ -10$^{8}$ Hz. In particular, dynamics- dependent suppression of peaks turned out to be very sensitive to the motion of 10$^{-4}$ s and 10$^{-5}$ s interfered with frequency of magic angle spinning and proton decoupling, respectively. It is also noteworthy that such dynamic feature is strongly dependent upon the manner of 2D crystalline packing: $^{13}$ C NMR peaks of monomeric bR yielded either highly broadened or completely suppressed signals, depending upon the type of $^{13}$ C-labeled amino-acid residues.

• Journal of the Korean Magnetic Resonance Society
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• v.12 no.2
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• pp.81-88
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• 2008

Solid HETCOR (Hetero-Correlation) requires homo-dipolar decoupling between proton spins during the evolution and the mixing period in 2D-NMR. There are two different ways of achieving it with pulse sequences. One is based on the multiple pulse (MP) sequence where thousands of intense radio frequency (rf) pulses are used to remove the homo-dipolar interaction between protons. The other is utilizing the so-called Lee-Goldburg (LG) off-resonance scheme where a continuous rf-irradiation is used. In this report, the advantage of one technique to the other, is analyzed. LG version is evaluated better in S/N and easier in setup procedure with the same experimental time.