Abstract Electron nuclear double resonance is a fundamental technique in EPR spectroscopy that directly detects hyperfine transitions of nuclei coupled to a paramagnetic center. Despite its wide use, spin-sensitivity and restricted spectral resolution in powder samples pose limitations of this technique in modern application fields of EPR. In this contribution we examine the performance of an ENDOR pulse sequence that utilizes a preparation scheme different from conventional Davies ENDOR. The scheme is based on electron-nuclear cross polarization (eNCP), which requires concomitant microwave (MW) and radio-frequency (RF) irradiation satisfying specific matching conditions between the MW and RF offsets and the hyperfine coupling. Changes in nuclear polarization generated during eNCP can be detected via a conventional ENDOR read-out sequence consisting of a RF ?-pulse followed by EPR-spin echo detection. Using 1H BDPA as a standard sample, we first examine the CP matching conditions by monitoring the depolarization of the electron spin magnetization. Subsequently, so-called CP-edited ENDOR spectra for different matching conditions are reported and analyzed based on the provided theoretical description of the time evolution of the spin density matrix during the experiment. The results demonstrate that CP-edited ENDOR provides additional information with respect to the sign of the hyperfine couplings. Furthermore, the sequence is less sensitive to nuclear saturation effects encountered in conventional ENDOR.
Stepwise Filtering of the Internal Layers of Dendrimersby Transverse-Relaxation-Edited NMR
Stepwise Filtering of the Internal Layers of Dendrimersby Transverse-Relaxation-Edited NMR
Luiz F. Pinto, Ricardo Riguera and Eduardo Fernandez-Megia
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja4059348/aop/images/medium/ja-2013-059348_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja4059348
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ipXC3MPLDn8
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07-30-2013 09:57 PM
Postdoc position in Warwick doing ENDOR-DNP
From The DNP-NMR Blog:
Postdoc position in Warwick doing ENDOR-DNP
The Magnetic Resonance Group in the Physics Department at the University of Warwick invites applications for a post-doctoral research fellow to work on the EPSRC-funded project "ENDOR-DNP". In addition to dynamic nuclear polarization (DNP), the group has a broad research program from high-field EPR to solid-state NMR.
Outstanding equipment is available for this research and you will develop and operate DNP spectrometers at both 14.1 and 3.4 T (600 MHz and 143 MHz). We already perform high-resolution NMR on both...
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05-14-2013 12:19 AM
[Question from NMRWiki Q&A forum] 2D NOESY filtered/edited experiments
2D NOESY filtered/edited experiments
what are the name for 2D NOESY filtered/edited experiments like F1fF2f, F1fF2e, F2f, F1eF2e in Bruker 700MHz ?.Here is the link of that paper which has above experimentshttp://www.ncbi.nlm.nih.gov/pubmed/14739639
Check if somebody has answered this question on NMRWiki QA forum
[NMR paper] Improved spin-echo-edited NMR diffusion measurements.
Improved spin-echo-edited NMR diffusion measurements.
Related Articles Improved spin-echo-edited NMR diffusion measurements.
J Magn Reson. 2001 Dec;153(2):273-6
Authors: Otto WH, Larive CK
The need for simple and robust schemes for the analysis of ligand-protein binding has resulted in the development of diffusion-based NMR techniques that can be used to assay binding in protein solutions containing a mixture of several ligands. As a means of gaining spectral selectivity in NMR diffusion measurements, a simple experiment, the gradient modified...
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11-19-2010 08:44 PM
High-resolution methyl edited GFT NMR experiments for protein resonance assignments a
High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination
Abstract Three-dimensional (3D) structure determination of proteins is benefitted by long-range distance constraints comprising the methyl groups, which constitute the hydrophobic core of proteins. However, in methyl groups (of Ala, Ile, Leu, Met, Thr and Val) there is a significant overlap of 13C and 1H chemical shifts. Such overlap can be resolved using the recently proposed (3,2)D HCCH-COSY, a G-matrix Fourier transform (GFT) NMR based experiment, which facilitates editing...
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09-18-2010 04:53 AM
High-resolution methyl edited GFT NMR experiments for protein resonance assignments a
High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination.
Related Articles High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination.
J Biomol NMR. 2010 Sep 14;
Authors: Jaipuria G, Thakur A, D'Silva P, Atreya HS
Three-dimensional (3D) structure determination of proteins is benefitted by long-range distance constraints comprising the methyl groups, which constitute the hydrophobic core of proteins. However, in methyl groups (of Ala, Ile,...
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09-15-2010 02:26 PM
[NMR paper] Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deute
Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS.
Related Articles Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS.
J Biomol NMR. 1993 Jan;3(1):121-6
Authors: Anglister J, Grzesiek S, Ren H, Klee CB, Bax A
At the concentration needed for NMR, the calcium-saturated form of calcineurin B dissolved in water shows resonance line widths that indicate aggregation of this protein. Although the line width or aggregation state can be...
Cross-polarisation edited ENDOR
Linear Mode
