Publication year: 2011 Source: Journal of Magnetic Resonance, Available online 22 September 2011
Paul R.*Murray, David*Collison, Simon*Daff, Nicola*Austin, Ruth*Edge, ...
A simple design for anin situ, three-electrode spectroelectrochemical cell is reported that can be used in commercial Q- and W-band (ca. 34 and 94 GHz, respectively) electron paramagnetic resonance (EPR) spectrometers, using standard sample tubing (1.0 and 0.5 mm inner diameter, respectively) and within variable temperature cryostat systems. The use of the cell is demonstrated by thein situgeneration of organic free radicals (quinones and diimines) in fluid and frozen media, transition metal ion radical anions, and on the enzyme nitric oxide synthase reductase domain (NOSrd), in which a pair of flavin radicals are generated. Graphical abstract
Highlights
? In situ EPR/ESR spectroelectrochemistry at high frequency. ? 3-electrode cells in standard Q- and W-band silica tubes. ? Variable temperature operation, including frozen solutions. ? Example operation on ubiquinone, bpipyridines and their platinum complexes, and a flavin protein.
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Chembiochem. 2011 Mar 29;
Authors: Crowley PB, Chow E, Papkovskaia T
Protein science is shifting towards experiments performed under native or native-like conditions. In-cell NMR spectroscopy for instance has the potential to reveal protein structure and dynamics inside cells. However, not all proteins can be studied by this technique. (15) N-labelled...
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03-31-2011 06:24 PM
[NMR paper] In-cell NMR spectroscopy.
In-cell NMR spectroscopy.
Related Articles In-cell NMR spectroscopy.
Methods Enzymol. 2005;394:17-41
Authors: Serber Z, Corsini L, Durst F, Dötsch V
The role of a protein inside a cell is determined by both its location and its conformational state. Although fluorescence techniques are widely used to determine the cellular localization of proteins in vivo, these approaches cannot provide detailed information about a protein's three-dimensional state. This gap, however, can be filled by NMR spectroscopy, which can be used to investigate both...
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11-24-2010 11:14 PM
In-Cell NMR Spectroscopy
In-Cell NMR Spectroscopy
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 17 November 2010</br>
Andres Y., Maldonado , David S., Burz , Alexander, Shekhtman</br>
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11-18-2010 06:16 PM
Plant Cell-Wall Cross-Links by REDOR NMR Spectroscopy.
Plant Cell-Wall Cross-Links by REDOR NMR Spectroscopy.
Related Articles Plant Cell-Wall Cross-Links by REDOR NMR Spectroscopy.
J Am Chem Soc. 2010 Oct 21;
Authors: Cegelski L, O'Connor RD, Stueber D, Singh M, Poliks B, Schaefer J
We present a new method that integrates selective biosynthetic labeling and solid-state NMR detection to identify in situ important protein cross-links in plant cell walls. We have labeled soybean cells by growth in media containing l-tyrosine and l-tyrosine, compared whole-cell and cell-wall (13)C CPMAS spectra, and...
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10-23-2010 05:48 PM
Plant Cell-Wall Cross-Links by REDOR NMR Spectroscopy
Plant Cell-Wall Cross-Links by REDOR NMR Spectroscopy
Lynette Cegelski, Robert D. O’Connor, Dirk Stueber, Manmilan Singh, Barbara Poliks and Jacob Schaefer
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja104827k/aop/images/medium/ja-2010-04827k_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja104827k
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/1kI0vIFK7eU
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10-22-2010 07:34 AM
[NMR thesis] Band 3 structure and function : [superscript]35 C1 NMR and topographical investigatio
Band 3 structure and function : 35 C1 NMR and topographical investigations
Kanes, Katherine J. (1989) Band 3 structure and function : 35 C1 NMR and topographical investigations. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-05302007-081241
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Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
David S Burz, Kaushik Dutta, David Cowburn & Alexander Shekhtman
We describe a high-throughput in-cell nuclear magnetic resonance (NMR)-based method for mapping the structural changes that accompany protein-protein interactions (STINT-NMR). The method entails sequentially expressing two (or more) proteins within a single bacterial cell in a time-controlled manner and monitoring the protein interactions using in-cell NMR spectroscopy. The resulting spectra provide a complete titration of the interaction and define...
Anin situelectrochemical cell for Q- and W-band EPR spectroscopy
Linear Mode
