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J Biomol NMR. 2018 Apr;70(4):205-209. doi: 10.1007/s10858-018-0181-6. Epub 2018 Apr 16.

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

Author information

1
Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, New York, NY, 10032, USA.
2
Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, New York, NY, 10032, USA. agp6@columbia.edu.

Abstract

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.

KEYWORDS:

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

PMID:
29663108
DOI:
10.1007/s10858-018-0181-6
[Indexed for MEDLINE]

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