Related ArticlesUltrafast Two-Dimensional NMR Relaxometry for Investigating Molecular Processes in Real Time.
Chemphyschem. 2014 Mar 13;
Authors: Ahola S, Telkki VV
Abstract
Nuclear spin-lattice (T1 ) and spin-spin (T2 ) relaxation times provide versatile information about the dynamics and structure of substances, such as proteins, polymers, porous media, and so forth. Multidimensional experiments increase the information content and resolution of NMR relaxometry, but they also multiply the measurement time. To overcome this issue, we present an efficient strategy for a single-scan measurement of a 2D T1 -T2 correlation map. The method shortens the experimental time by one to three orders of magnitude as compared to the conventional method, offering an unprecedented opportunity to study molecular processes in real-time. We demonstrate that, despite the tremendous speed-up, the T1 -T2 correlation maps determined by the single-scan method are in good agreement with the maps measured by the conventional method. The concept of the single-scan T1 -T2 correlation experiment is applicable to a broad range of other multidimensional relaxation and diffusion experiments.
PMID: 24634359 [PubMed - as supplied by publisher]
[NMR paper] Fast Real-Time NMR Methods for Characterizing Short-Lived Molecular States.
Fast Real-Time NMR Methods for Characterizing Short-Lived Molecular States.
Fast Real-Time NMR Methods for Characterizing Short-Lived Molecular States.
Chemphyschem. 2013 Jul 15;
Authors: Rennella E, Brutscher B
Abstract
The characterization of both the structure and the conformational dynamics of biological macromolecules, namely proteins and nucleic acids, is required for understanding the molecular mechanisms underlying physiological function and disease. Molecular dynamics involves the transient departure from the ground-state...
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NMR spectroscopy in environmental research: From molecular interactions to global processes
NMR spectroscopy in environmental research: From molecular interactions to global processes
Publication year: 2011
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 58, Issues 3–4</br>
André J. Simpson, David J. McNally, Myrna J. Simpson</br>
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Monitoring Mechanistic Details in the Synthesis of Pyrimidines via Real-Time, Ultrafast Multidimensional NMR Spectroscopy
Monitoring Mechanistic Details in the Synthesis of Pyrimidines via Real-Time, Ultrafast Multidimensional NMR Spectroscopy
Zulay D. Pardo, Gregory L. Olsen, Mari?a Encarnacio?n Ferna?ndez-Valle, Lucio Frydman, Roberto Marti?nez-A?lvarez and Antonio Herrera
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja210154g/aop/images/medium/ja-2011-10154g_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja210154g
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/tEFGGh16-DU
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Li Ion Diffusion in the Anode Material Li12Si7: Ultrafast Quasi-1D Diffusion and Two Distinct Fast 3D Jump Processes Separately Revealed by 7Li NMR Relaxometry
Li Ion Diffusion in the Anode Material Li12Si7: Ultrafast Quasi-1D Diffusion and Two Distinct Fast 3D Jump Processes Separately Revealed by 7Li NMR Relaxometry
Alexander Kuhn, Puravankara Sreeraj, Rainer Po?ttgen, Hans-Dieter Wiemho?fer, Martin Wilkening and Paul Heitjans
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2020108/aop/images/medium/ja-2011-020108_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2020108
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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06-28-2011 04:32 AM
[NMR paper] Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic eve
Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.
Related Articles Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.
J Am Chem Soc. 2005 Jun 8;127(22):8014-5
Authors: Schanda P, Brutscher B
We demonstrate for different protein samples that 2D 1H-15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle...
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11-25-2010 08:21 PM
[NMR paper] Protein folding studied by real-time NMR spectroscopy.
Protein folding studied by real-time NMR spectroscopy.
Related Articles Protein folding studied by real-time NMR spectroscopy.
Methods. 2004 Sep;34(1):65-74
Authors: Zeeb M, Balbach J
Real-time NMR spectroscopy developed to a generally applicable method to follow protein folding reactions. It combines the access to high resolution data with kinetic experiments allowing very detailed insights into the development of the protein structure during different steps of folding. The present review concentrates mainly on the progress of real-time NMR...
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[NMR paper] Following protein folding in real time using NMR spectroscopy.
Following protein folding in real time using NMR spectroscopy.
Related Articles Following protein folding in real time using NMR spectroscopy.
Nat Struct Biol. 1995 Oct;2(10):865-70
Authors: Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM
The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative...
Ultrafast Two-Dimensional NMR Relaxometry for Investigating Molecular Processes in Real Time.
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