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

Lookup NU author(s): Professor Steve Homans

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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.

Publication metadata

Author(s): Burnley BT, Kalverda AP, Paisey SJ, Berry A, Homans SW

Publication type: Article

Publication status: Published

Journal: Journal of Biomolecular NMR

Year: 2007

Volume: 39

Issue: 3

Pages: 239-245

ISSN (print): 0925-2738

ISSN (electronic): 1573-5001

Publisher: Springer Netherlands

URL: http://dx.doi.org/10.1007/s10858-007-9192-4

DOI: 10.1007/s10858-007-9192-4

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