Journal
JOURNAL OF MAGNETIC RESONANCE
Volume 143, Issue 2, Pages 423-426Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/jmre.2000.2022
Keywords
TROSY; protein dynamics; NMR; relaxation
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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.
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