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

Hadamard NMR spectroscopy for relaxation measurements of large (>35 kDa) proteins
B. Tom Burnley, Arnout P. Kalverda, Stephen J. Paisey, Alan Berry and Steve W. Homans
Journal of Biomolecular NMR; 2007; 39(3) pp 239 - 245

Abstract:

Here we present a suite of pulse sequences for the measurement of 15N T1, T1ρ 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.
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