Publication year: 2010 Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 17 November 2010
Andres Y., Maldonado , David S., Burz , Alexander, Shekhtman
Anin situelectrochemical cell for Q- and W-band EPR spectroscopy
Anin situelectrochemical cell for Q- and W-band EPR spectroscopy
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 22 September 2011</br>
Paul R.*Murray, David*Collison, Simon*Daff, Nicola*Austin, Ruth*Edge, ...</br>
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....
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09-24-2011 06:04 AM
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...
[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
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
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...
In-Cell NMR Spectroscopy
Linear Mode
