期刊
JOURNAL OF MAGNETIC RESONANCE
卷 182, 期 2, 页码 339-342出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jmr.2006.06.028
关键词
proton driven spin diffusion; magic angle spinning; CODEX; proteins; structure; dynamics; isotope enrichment
As demonstrated by means of the one-dimensional solid-state MAS exchange experiment (CODEX), the rate of the proton driven spin diffusion between backbone N-15 nuclei in totally enriched protein depends strongly on the magic angle spinning (MAS) frequency: spin diffusion at MAS frequency 16 kHz is about 4-5 times slower as compared to that at MAS frequency I kHz which is due to the averaging of the homo- and hetero-nuclear dipolar interactions by MAS. It is important that even at the highest MAS frequencies used in our experiments the spin diffusion rate is comparable or larger than typical values of the spin-lattice relaxation rates of backbone nitrogens in solid proteins. Thus, the precise quantitative analysis of N-15 T-1's in totally enriched solid proteins may lead to wrong quantitative results. On the other hand, the effectiveness of the N-15-N-15 correlation and structure determination experiments making use of N-15-N-15 distances can be increased by decreasing the MAS frequency as far as possible, which is counter intuitive to the commonly applied fast MAS conditions in order to reduce the dipolar-broadened line widths for increased spectral resolution. (c) 2006 Elsevier Inc. All rights reserved.
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