Hadamard NMR spectroscopy for relaxation measurements of large (>35 kDa) proteins.
J. Biomol. NMR. 2007 Nov;39(3):239-45. doi:10.1007/s10858-007-9192-4. Epub 2007 Sep 20
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摘要
Here we present a suite of pulse sequences for the measurement of (15)N T(1), T(1rho) and NOE data that combine traditional 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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基因功能
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原始数据
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文献解读
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