Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 49, Issue 1, Pages 9-15Publisher
SPRINGER
DOI: 10.1007/s10858-010-9461-5
Keywords
BEST; Fast NMR; Longitudinal-relaxation enhancement; Protein; Sensitivity; TROSY
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Funding
- Commissariat a l'Energie Atomique
- Centre National de la Recherche Scientifique
- University of Grenoble
- French research agency [ANR 08-BLAN-210]
- European Commission [261863]
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Experimental sensitivity remains a major drawback for the application of NMR spectroscopy to fragile and low concentrated biomolecular samples. Here we describe an efficient polarization enhancement mechanism in longitudinal-relaxation enhanced fast-pulsing triple-resonance experiments. By recovering undetectable H-1 polarization originating from longitudinal relaxation during the pulse sequence, the steady-state N-15 polarization becomes enhanced by up to a factor of similar to 5 with respect to thermal equilibrium yielding significant sensitivity improvements compared to conventional schemes. The benefits of BEST-TROSY experiments at high magnetic field strength are illustrated for various protein applications, but they will be equally useful for other protonated macromolecular systems.
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