Related ArticlesPractical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology.
Methods. 2018 Jun 28;:
Authors: Caro JA, Wand AJ
Abstract
Pressure and temperature are the two fundamental variables of thermodynamics. Temperature and chemical perturbation are central experimental tools for the exploration of macromolecular structure and dynamics. Though it has long been recognized that hydrostatic pressure offers a complementary and often unique view of macromolecular structure, stability and dynamics, it has not been employed nearly as much. For solution NMR applications the limited use of high-pressure is undoubtedly traced to difficulties of employing pressure in the context of modern multinuclear and multidimensional NMR. Limitations in pressure tolerant NMR sample cells have been overcome and enable detailed studies of macromolecular energy landscapes, hydration, dynamics and function. Here we review the practical considerations for studies of biological macromolecules at elevated pressure, with a particular emphasis on applications in protein biophysics and structural biology.
PMID: 29964175 [PubMed - as supplied by publisher]
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell [Biophysics and Computational Biology]
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell
Cyril Charlier, T. Reid Alderson, Joseph M. Courtney, Jinfa Ying, Philip Anfinrud, Adriaan Bax...
Date: 2018-05-01
In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded and unfolded states, their thermodynamic equilibrium can be altered by varying the hydrostatic pressure. Using a pressure-sensitized mutant of ubiquitin, we demonstrate that rapidly switching the...
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Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy [Biophysics and Computational Biology]
Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy
Yuki Toyama, Hanaho Kano, Yoko Mase, Mariko Yokogawa, Masanori Osawa, Ichio Shimada...
Date: 2018-04-10
Ethanol consumption leads to a wide range of pharmacological effects by acting on the signaling proteins in the human nervous system, such as ion channels. Despite its familiarity and biological importance, very little is known about the molecular mechanisms underlying the ethanol action, due to extremely weak binding affinity and... Read More
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04-11-2018 12:49 AM
Modular 129Xe NMR biosensor for MRI applications [Biophysics and Computational Biology]
Modular 129Xe NMR biosensor for MRI applications
Rose, H. M., Witte, C., Rossella, F., Klippel, S., Freund, C., Schroder, L....
Date: 2014-08-12
Magnetic resonance imaging (MRI) is seriously limited when aiming for visualization of targeted contrast agents. Images are reconstructed from the weak diamagnetic properties of the sample and require an abundant molecule like water as the reporter. Micromolar to millimolar concentrations of conventional contrast agents are needed to generate image contrast,... Read More
PNAS:
Number: 32
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08-13-2014 07:49 AM
[NMR paper] Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.
Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.
Related Articles Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.
Protein Eng Des Sel. 2013 Mar 22;
Authors: Ogura K, Kobashigawa Y, Saio T, Kumeta H, Torikai S, Inagaki F
Abstract
Recently, the hydrostatic pressure refolding method was reported as a practical tool for solubilizing and refolding proteins from inclusion bodies; however, there have been...
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03-26-2013 01:30 PM
Practical aspects of high-sensitivity multidimensional 13C MAS NMR spectroscopy of perdeuterated proteins
Practical aspects of high-sensitivity multidimensional 13C MAS NMR spectroscopy of perdeuterated proteins
April 2012
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 217</br>
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The double nucleus enhanced recoupling (DONER) experiment employs simultaneous irradiation of protons and deuterons to promote spin diffusion processes in a perdeuterated protein. This results in 4–5times higher sensitivity in 2D 13C–13C correlation experiments as compared to PDSD . Here, a quantitative comparison of PDSD, 1H-DARR, 2H-DARR, and 1H+ 2H DONER has been...
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02-03-2013 10:13 AM
Practical Aspects of High-Sensitivity Multidimensional 13C MAS NMR Spectroscopy of Perdeuterated Proteins
Practical Aspects of High-Sensitivity Multidimensional 13C MAS NMR Spectroscopy of Perdeuterated Proteins
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Ümit Akbey, Barth-Jan van Rossum, Hartmut Oschkinat</br>
The double nucleus enhanced recoupling (DONER) experiment employs simultaneous irradiation of protons and deuterons to promote spin diffusion processes in a perdeuterated protein. This results in 4-5 times higher sensitivity in 2D 13C-13C correlation experiments as compared to PDSD. Here, a quantitative comparison of PDSD, 1H-DARR, 2H-DARR, and...
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03-09-2012 09:16 AM
Practical Aspects of High-Sensitivity MultidimensionalC MAS NMR Spectroscopy of Perdeuterated Proteins
Practical Aspects of High-Sensitivity MultidimensionalC MAS NMR Spectroscopy of Perdeuterated Proteins
Publication year: 2012
Source: Journal of Magnetic Resonance, Available online 1 March 2012</br>
Ümit*Akbey, Barth-Jan*van Rossum, Hartmut*Oschkinat</br>
Thedouble nucleus enhanced recoupling(DONER) experiment employs simultaneous irradiation of protons and deuterons to promote spin diffusion processes in a perdeuterated protein. This results in 4-5 times higher sensitivity in 2DC-C correlation experiments as compared to PDSD.Here, a quantitative comparison of PDSD,H-DARR,H-DARR,...
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03-01-2012 11:03 PM
Structural Biology- Practical NMR Applications-Quincy Teng
Structural Biology-Practical NMR Applications-Quincy Teng
I have just seen this book and have had time to skim it, seems like an excellent book to base an upper level undergrad or a grad course on, much easier to read than Cavanaugh and includes questions as well as learning goals for each section.
Has anyone else had a chance to go through this book?