Journal of Biomolecular NMR

, Volume 70, Issue 4, pp 205–209 | Cite as

TROSY pulse sequence for simultaneous measurement of the 15N R1 and {1H}–15N NOE in deuterated proteins

  • Paul A. O’Brien
  • Arthur G. PalmerIII


A TROSY-based NMR experiment is described for simultaneous measurement of the 15N longitudinal relaxation rate constant R1 and the {1H}–15N nuclear Overhauser enhancement. The experiment is based on the observation that the TROSY mixing pulse sequence element symmetrically exchanges 1H and 15N magnetizations. The accuracy of the proposed technique is validated by comparison to independent measurements of both relaxation parameters for the protein ubiquitin. The simultaneous experiment is approximately 20–33% shorter than conventional sequential measurements.


Dynamics Longitudinal relaxation Nuclear Overhauser enhancement Protein Spin–lattice relaxation TROSY 



Support from National Institutes of Health Grants R01 GM050291 (A.G.P.) and T32 GM008281 (P.A.O.) is acknowledged gratefully. We thank Mark Rance (University of Cincinnati) for helpful discussions. Some of the work presented here was conducted at the Center on Macromolecular Dynamics by NMR Spectroscopy located at the New York Structural Biology Center, supported by a Grant from the NIH National Institute of General Medical Sciences (P41 GM118302). A.G.P. is a member of the New York Structural Biology Center.

Supplementary material

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© Springer Science+Business Media B.V., part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiophysicsColumbia UniversityNew YorkUSA

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