Abstract
Nuclear magnetic resonance (NMR) studies have benefited tremendously from the steady increase in the strength of magnetic fields. Spectacular improvements in both sensitivity and resolution have enabled the investigation of molecular systems of rising complexity. At very high fields, this progress may be jeopardized by line broadening, which is due to chemical exchange or relaxation by chemical shift anisotropy. In this work, we introduce a two-field NMR spectrometer designed for both excitation and observation of nuclear spins in two distinct magnetic fields in a single experiment. NMR spectra of several small molecules as well as a protein were obtained, with two dimensions acquired at vastly different magnetic fields. Resonances of exchanging groups that are broadened beyond recognition at high field can be sharpened to narrow peaks in the low-field dimension. Two-field NMR spectroscopy enables the measurement of chemical shifts at optimal fields and the study of molecular systems that suffer from internal dynamics, and opens new avenues for NMR spectroscopy at very high magnetic fields.
PMID: 27417269 [PubMed - as supplied by publisher]
Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
J Biomol NMR. 2011 Mar 18;
Authors: Bouvignies G, Vallurupalli P, Cordes MH, Hansen DF, Kay LE
A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated 'invisible' protein states that exchange...
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03-23-2011 05:41 PM
Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy
Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy
Abstract A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated â??invisibleâ?? protein states that exchange with a â??visibleâ?? ground state on the millisecond time-scale. The utility of the approach is demonstrated with an application to an I58D mutant of the Pfl6 Cro protein that undergoes exchange between the native, folded state and a cold...
Recovering lost magnetization: polarization enhancement in biomolecular NMR
Recovering lost magnetization: polarization enhancement in biomolecular NMR
Abstract 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 1H polarization originating from longitudinal relaxation during the pulse sequence, the steady-state 15N polarization becomes enhanced by up to a factor of ~5 with respect to thermal...
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12-31-2010 08:38 PM
Recovering lost magnetization: polarization enhancement in biomolecular NMR.
Recovering lost magnetization: polarization enhancement in biomolecular NMR.
Recovering lost magnetization: polarization enhancement in biomolecular NMR.
J Biomol NMR. 2010 Dec 30;
Authors: Favier A, Brutscher B
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 (1)H polarization...
Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
D. Flemming Hansen, Pramodh Vallurupalli and Lewis E. Kay
Journal of Biomolecular NMR; 2008; 41(3); pp 113 - 120
Abstract:
Currently the main focus of structural biology is the determination of static three-dimensional representations of biomolecules that for the most part correspond to low energy (ground state) conformations. However, it is becoming increasingly well recognized that higher energy structures often play important roles in function as well. Because these conformers...