Boosting the resolution of low-field $$^{15}\hbox {N}$$15N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR
Boosting the resolution of low-field $$^{15}\hbox {N}$$15N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR
Abstract
Improving our understanding of nanosecond motions in disordered proteins requires the enhanced sampling of the spectral density function obtained from relaxation at low magnetic fields. High-resolution relaxometry and two-field NMR measurements of relaxation have, so far, only been based on the recording of one- or two-dimensional spectra, which provide insufficient resolution for challenging...
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02-29-2020 09:52 PM
[NMR paper] Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy.
Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy.
Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy.
Methods. 2018 Jan 13;:
Authors: Gibbs EB, Kriwacki RW
Abstract
Nuclear magnetic resonance spectroscopy (NMR) is a powerful technique for characterizing the structural and dynamic properties of intrinsically disordered proteins and protein regions (IDPs &...
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01-18-2018 12:41 PM
Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy
Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy
Publication date: Available online 16 January 2018
Source:Methods</br>
Author(s): E.B. Gibbs, R.W. Kriwacki</br>
Nuclear magnetic resonance spectroscopy (NMR) is a powerful technique for characterizing the structural and dynamic properties of intrinsically disordered proteins and protein regions (IDPs & IDRs). However, the application of NMR to IDPs has been limited by poor chemical shift dispersion in two-dimensional (2D) 1H-15N...
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01-17-2018 07:00 PM
[NMR paper] Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation.
Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation.
Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation.
Prog Nucl Magn Reson Spectrosc. 2017 Nov;102-103:43-60
Authors: Salvi N, Abyzov A, Blackledge M
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful experimental approaches for investigating the conformational behaviour of intrinsically disordered proteins (IDPs). IDPs represent a significant...
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11-22-2017 02:01 PM
Atomic Resolution Conformational Dynamics of Intrinsically Disordered Proteins from NMR Spin Relaxation
Atomic Resolution Conformational Dynamics of Intrinsically Disordered Proteins from NMR Spin Relaxation
Publication date: Available online 10 July 2017
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Nicola Salvi, Anton Abyzov, Martin Blackledge</br>
Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful experimental approaches for investigating the conformational behavior of intrinsically disordered proteins (IDPs). IDPs represent a significant fraction of all proteomes, and, despite their importance for...
15N detection harnesses the slow relaxation property of nitrogen: Delivering enhanced resolution for intrinsically disordered proteins - pnas.org
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