Köckenberger, W. and J. Matysik, Hyperpolarization Methods and Applications in NMR, in Encyclopedia of Spectroscopy and Spectrometry (Second Edition), L. Editor-in-Chief: John, Editor. 2010, Academic Press: Oxford. p. 963-970.
Nuclear magnetic resonance (NMR) is a well known and versatile spectroscopic and analytical technique. Its enormous success is due to its capacity to determine structures of molecules and proteins in solutions and amorphous solids, to measure local mobilities, to provide information on reaction mechanisms, and to construct three-dimensional images. The main constraints of NMR are its limitation to microsecond time resolution and the low sensitivity. The latter problem is caused by the weak magnetic properties of nuclei and a resulting unfavorable Boltzmann distribution occurring under equilibrium conditions. Therefore, several methods have been developed to produce non-Boltzmann nuclear spin states leading to hyperpolarization and enhanced sensitivity. These hyperpolarization methods induce spin-chemical processes that overcome the Boltzmann equilibrium of the nuclear spins. Under these conditions, signals enhanced to a factor of more than 10 000 are observed. Hyperpolarization methods use light, microwaves, or chemical reactions and, therefore, link different forms of spectroscopy.
Long-Range Proton-Carbon Coupling Constants: NMR methods and applications
Long-Range Proton-Carbon Coupling Constants: NMR methods and applications
Publication date: Available online 20 July 2013
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Teodor Parella , Juan Félix Espinosa</br>
A general review of novel NMR methods to measure heteronuclear long-range proton-carbon coupling constants ( n J CH ; n>1) in small molecules is made. NMR experiments are classified in terms of NMR pulse scheme and cross-peak nature. A discussion about simplicity, general applicability and accuracy for each...
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07-20-2013 11:27 AM
Dynamic Nuclear Hyperpolarization in Liquids
From The DNP-NMR Blog:
Dynamic Nuclear Hyperpolarization in Liquids
Günther, U., Dynamic Nuclear Hyperpolarization in Liquids, in Modern NMR Methodology, H. Heise and S. Matthews, Editors. 2013, Springer Berlin Heidelberg. p. 23-69.
http://dx.doi.org/10.1007/128_2011_229
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07-18-2013 12:39 AM
[NMR paper] Biomolecular magic-angle spinning solid-state NMR: recent methods and applications.
Biomolecular magic-angle spinning solid-state NMR: recent methods and applications.
Related Articles Biomolecular magic-angle spinning solid-state NMR: recent methods and applications.
Curr Opin Biotechnol. 2013 Mar 4;
Authors: Goldbourt A
Abstract
The link of structure and dynamics of biomolecules and their complexes to their function and to many cellular processes has driven the quest for their detailed characterization by a variety of biophysical techniques. Magic-angle spinning solid-state nuclear magnetic resonance spectroscopy...
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03-14-2013 10:05 PM
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Abstract We present new NMR methods to measure slow translational diffusion coefficients of biomolecules. Like the heteronuclear stimulated echo experiment (XSTE), these new methods rely on the storage of information about spatial localization during the diffusion delay as longitudinal polarization of nuclei with long T1 such as nitrogen-15. The new BEST-XSTE sequence combines features of Band-selective Excitation Short-Transient (BEST) and XSTE methods. By...
Using NMR to study fast dynamics in proteins: methods and applications.
Using NMR to study fast dynamics in proteins: methods and applications.
Related Articles Using NMR to study fast dynamics in proteins: methods and applications.
Curr Opin Pharmacol. 2010 Oct 6;
Authors: Sapienza PJ, Lee AL
Proteins exist not as singular structures with precise coordinates, but rather as fluctuating bodies that move rapidly through an enormous number of conformational substates. These dynamics have important implications for understanding protein function and for structure-based drug design. NMR spectroscopy is particularly well...
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10-12-2010 02:52 PM
ICMRBS founder’s medal 2006: Biological solid-state NMR, methods and applications
ICMRBS founder’s medal 2006: Biological solid-state NMR, methods and applications
Marc Baldus
Journal of Biomolecular NMR; 2007; 39(1); pp 73-86
Abstract:
Solid-state NMR (ssNMR) provides increasing possibilities to study structure and dynamics of biomolecular systems. Our group has been interested in developing ssNMR-based approaches that are applicable to biomolecules of increasing molecular size and complexity without the need of specific isotope-labelling. Methodological aspects ranging from spectral assignments to the indirect detection of proton–proton contacts in...