In-Cell NMR and EPR Spectroscopy of Biomacromolecules.
Angew Chem Int Ed Engl. 2014 Jul 28;
Authors: Hänsel R, Luh LM, Corbeski I, Trantirek L, Dötsch V
Abstract
The dream of cell biologists is to be able to watch biological macromolecules perform their duties in the intracellular environment of live cells. Ideally, the observation of both the location and the conformation of these macromolecules with biophysical techniques is desired. The development of many fluorescence techniques, including superresolution fluorescence microscopy, has significantly enhanced our ability to spot proteins and other molecules in the crowded cellular environment. However, the observation of their structure and conformational changes while they attend their business is still very challenging. In principle, NMR and EPR spectroscopy can be used to investigate the conformation and dynamics of biological macromolecules in living cells. The development of in-cell magnetic resonance techniques has demonstrated the feasibility of this approach. Herein we review the different techniques with a focus on liquid-state in-cell NMR spectroscopy, provide an overview of applications, and discuss the challenges that lie ahead.
PMID: 25070284 [PubMed - as supplied by publisher]
[NMR paper] Chemical exchange in biomacromolecules: Past, present, and future
Chemical exchange in biomacromolecules: Past, present, and future
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): Arthur G. Palmer III</br>
The perspective reviews quantitative investigations of chemical exchange phenomena in proteins and other biological macromolecules using NMR spectroscopy, particularly relaxation dispersion methods. The emphasis is on techniques and applications that quantify the populations, interconversion kinetics, and structural features of sparsely populated conformational states in equilibrium...
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03-22-2014 01:28 AM
[NMR paper] NMR Spectroscopy on Domain Dynamics in Biomacromolecules.
NMR Spectroscopy on Domain Dynamics in Biomacromolecules.
Related Articles NMR Spectroscopy on Domain Dynamics in Biomacromolecules.
Prog Biophys Mol Biol. 2013 May 15;
Authors: Shapiro YE
Abstract
Domain dynamics in biomacromolecules is currently an area of intense research because of its importance for understanding the huge quantity of available data relating the structure and function of proteins and nucleic acids. Control of structural flexibility is essential for the proper functioning of the biomacromolecules. Biophysical...
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05-21-2013 02:34 PM
In-cell NMR spectroscopy
In-cell NMR spectroscopy
October 2011
Publication year: 2011
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 59, Issue 3</br>
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12-15-2012 09:51 AM
In-cell NMR spectroscopy
In-cell NMR spectroscopy
October 2011
Publication year: 2011
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 59, Issue 3</br>
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12-01-2012 06:10 PM
In-cell NMR spectroscopy
In-cell NMR spectroscopy
Publication year: 2011
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 59, Issue 3</br>
Andres Y. Maldonado, David S. Burz, Alexander Shekhtman</br>
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03-09-2012 09:16 AM
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
[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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