2D and 3D TROSY-enhanced NOESY of 15N labeled proteins

Guang Zhu, Youlin Xia, Kong Hung Sze, Xiangzhong Yan

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

Recently, several TROSY-based experiments have been designed for backbone chemical shift assignment and measurement of the NOEs of 2H, 13C and 15N labeled proteins. Here, we present TROSY-enhanced NOESY experiments, namely the 2D S3E-NOESY-S3E, 3D TROSY-NOESY-S3E and S3E-NOESY-TROSY experiments. These experiments use the spin-state selective excitation method (S3E), and have the TROSY effect in all the indirectly and directly detected dimensions, and so provide optimal resolution for amide protons. The first two experiments provide an additional useful feature in that the diagonal peaks of the amide proton region are cancelled or greatly reduced, allowing clear identification of NOE cross peaks that are close to diagonal peaks.

Original languageEnglish (US)
Pages (from-to)377-381
Number of pages5
JournalJournal of biomolecular NMR
Volume14
Issue number4
DOIs
StatePublished - 1999

Bibliographical note

Funding Information:
This work is supported by grants from the Research Grant Council of Hong Kong (HKUST6197/97M and HKUST6038/98M). We also thank Dr. Mingjie Zhang for providing the 15N labeled calmodulin, and Dr. D.K. Smith for critical discussions. The Hong Kong Biotechnology Research Institute is acknowledged for the purchase of the 750 MHz NMR spectrometer.

Keywords

  • N labeled proteins
  • NOESY
  • TROSY

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