Journal of Biomolecular NMR

, Volume 39, Issue 3, pp 239–245 | Cite as

Hadamard NMR spectroscopy for relaxation measurements of large (>35 kDa) proteins

  • B. Tom Burnley
  • Arnout P. Kalverda
  • Stephen J. Paisey
  • Alan Berry
  • Steve W. Homans
Article

Abstract

Here we present a suite of pulse sequences for the measurement of 15N T1,   T and NOE data that combine traditional TROSY-based pulse sequences with band-selective Hadamard frequency encoding. The additive nature of the Hadamard matrix produces much reduced resonance overlap without the need for an increase in the dimensionality of the experiment or a significant decrease in the signal to noise ratio. We validate the accuracy of these sequences in application to ubiquitin and demonstrate their utility for relaxation measurements in Escherichia coli Class II fructose 1,6-bisphosphate aldolase (FBP-aldolase), a 358 residue 78 kDa dimeric enzyme.

Supplementary material

10858_2007_9192_MOESM1_ESM.doc (267 kb)
ESM1 (DOC 267 KB)

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Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • B. Tom Burnley
    • 1
  • Arnout P. Kalverda
    • 1
  • Stephen J. Paisey
    • 1
  • Alan Berry
    • 1
  • Steve W. Homans
    • 1
  1. 1.Astbury Centre for Structural Molecular BiologyUniversity of LeedsLeedsUK

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