Protein Dynamics Measurements by TROSY-Based NMR Experiments

Guang Zhu, Youlin Xia, Linda K. Nicholson, Kong Hung Sze

Research output: Contribution to journalEditorialpeer-review

133 Scopus citations

Abstract

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 15 N nuclei. In our proposed sequences, the INEPT sequence is eliminated and the PEP sequence is replaced by the ST2-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 15 N-labeled Xenopus laevis calcium-bound calmodulin sample on a 750-MHz spectrometer at 5°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.

Original languageEnglish (US)
Pages (from-to)423-426
Number of pages4
JournalJournal of Magnetic Resonance
Volume143
Issue number2
DOIs
StatePublished - Apr 2000

Bibliographical note

Funding Information:
This work is supported by grants from the Research Grant Council of Hong Kong (HKUST6197/97M, HKUST6038/98M, and HKUST6199/99M). The Hong Kong Biotechnology Research Institute is acknowledged for the purchase of the 750-MHz NMR spectrometer. LKN acknowledges support from the National Science Foundation (MCB-9808727) and the National Institutes of Health (1 R01 CA77478-01).

Keywords

  • NMR
  • Protein dynamics
  • Relaxation
  • TROSY

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