[NMR paper] Longitudinal Spin Order Labeling on Multiple Quantum Coherences Enables NMR Analysis of Intrinsically Disordered Proteins at Ultrahigh Resolution
Longitudinal Spin Order Labeling on Multiple Quantum Coherences Enables NMR Analysis of Intrinsically Disordered Proteins at Ultrahigh Resolution
Intrinsically disordered proteins (IDPs) play an important role in cell signaling, and NMR is well-suited to study conformational ensembles and dynamics of IDPs. However, the intrinsic flexibility of IDPs often results in severe spectral overlap, which hampers accurate NMR data analysis. By labeling the longitudinal spin order of an ? proton (i.e., H^(?)(z)) on multiple quantum coherences of backbone nuclei (e.g., N(y)C'(x)C^(?)(y)), we were able...
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09-21-2021 06:03 PM
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] 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...
[NMR paper] Describing intrinsically disordered proteins at atomic resolution by NMR.
Describing intrinsically disordered proteins at atomic resolution by NMR.
Related Articles Describing intrinsically disordered proteins at atomic resolution by NMR.
Curr Opin Struct Biol. 2013 Mar 29;
Authors: Jensen MR, Ruigrok RW, Blackledge M
Abstract
There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from...
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04-03-2013 08:22 PM
Describing intrinsically disordered proteins at atomic resolution by NMR
Describing intrinsically disordered proteins at atomic resolution by NMR
Available online 29 March 2013
Publication year: 2013
Source:Current Opinion in Structural Biology</br>
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There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from nuclear magnetic resonance spectroscopy are presented. Ensemble approaches are particularly well adapted to map the...
Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation - ScienceDirect.com
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