期刊
JOURNAL OF MAGNETIC RESONANCE
卷 143, 期 2, 页码 423-426出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/jmre.2000.2022
关键词
TROSY; protein dynamics; NMR; relaxation
The described TROSY-based experiments for investigating backbone dynamics of proteins make it possible to elucidate internal motions in large proteins via measurements of T-1, T-2, and NOE of backbone N-15 nuclei. In our proposed sequences, the INEPT sequence is eliminated and the PEP sequence is replaced by the STZ-PT sequence from the HSQC-based experiments. This has the benefit of shortening the pulse sequences by 5.4 ms (= 1/2J) and results in an increase in the intrinsic sensitivity of the proposed TROSY-based experiments. The TROSY-based experiments are on average of 13% more sensitive than the corresponding HSQC-based experiments on a uniformly N-15-labeled Xenopus laevis calcium-bound calmodulin sample on a 750-MHz spectrometer at 5 degrees C. The amide proton linewidths of the TROSY-based experiments are 2-13 Hz narrower than those of the HSQC experiments. More sensitivity gain and higher resolution are expected if the protein sample is deuterated. (C) 2000 Academic Press.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据