NMR represents a key spectroscopic technique that contributes to the emerging field of highly flexible, intrinsically disordered proteins (IDPs) or protein regions (IDRs) that lack a stable three-dimensional structure. A set of exclusively heteronuclear NMR experiments tailored for proline residues, highly abundant in IDPs/IDRs, are presented here. They provide a valuable complement to the widely used approach based on amide proton detection, filling the gap introduced by the lack of amide...
[NMR paper] Zooming into the Interaction of ?-synuclein with Calcium Ions through Exclusively Heteronuclear NMR Experiments.
Zooming into the Interaction of ?-synuclein with Calcium Ions through Exclusively Heteronuclear NMR Experiments.
Related Articles Zooming into the Interaction of ?-synuclein with Calcium Ions through Exclusively Heteronuclear NMR Experiments.
Angew Chem Int Ed Engl. 2020 Jul 31;:
Authors: Pontoriero L, Schiavina M, Murrali MG, Pierattelli R, Felli IC
Abstract
Many properties of intrinsically disordered proteins (IDPs) or protein regions (IDRs) are expected to be modulated by the nature of amino acid side chains as well as by...
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08-01-2020 02:01 PM
Dispersion from C α or N H : 4D experiments for backbone resonance assignment of intrinsically disordered proteins
Dispersion from C α or N H : 4D experiments for backbone resonance assignment of intrinsically disordered proteins
Abstract
Resonance assignment of intrinsically disordered proteins is remarkably challenging due to scant chemical shift dispersion arising from conformational heterogeneity. The challenge is even greater if repeating segments are present in the amino acid sequence. To forward unambiguous resonance assignment of intrinsically disordered proteins, we present iHACANCO, HACACON and (HACA)CONCAHA, three Hα-detected 4D experiments with Cα...
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02-29-2020 09:52 PM
[NMR paper] Sensitivity-enhanced Four-dimensional Amide-amide Correlation NMR Experiments for Sequential Assignment of Proline-rich Disordered Proteins.
Sensitivity-enhanced Four-dimensional Amide-amide Correlation NMR Experiments for Sequential Assignment of Proline-rich Disordered Proteins.
Sensitivity-enhanced Four-dimensional Amide-amide Correlation NMR Experiments for Sequential Assignment of Proline-rich Disordered Proteins.
J Am Chem Soc. 2018 Feb 28;:
Authors: Wong LE, Maier J, Wienands J, Becker S, Griesinger C
Abstract
Proline is prevalent in intrinsically disordered proteins (IDPs). NMR assignment of proline-rich IDPs is a challenge due to low dispersion of chemical...
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03-01-2018 09:20 PM
Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water
From The DNP-NMR Blog:
Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water
p.p1 {margin: 0.0px 0.0px 0.0px 36.0px; text-indent: -36.0px; font: 12.0px Helvetica}
Kurzbach, D., et al., Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water. Angew. Chem. Int. Ed., 2017. 56(1): p. 389-392.
http://dx.doi.org/10.1002/anie.201608903
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02-28-2017 12:02 AM
[NMR paper] Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water
Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water
Hyperpolarized water can selectively enhance NMR signals of rapidly exchanging protons in osteopontin (OPN), a metastasis-associated intrinsically disordered protein (IDP), at near-physiological pH and temperature. The transfer of magnetization from hyperpolarized water is limited to solvent-exposed residues and therefore selectively enhances signals in 1H-15N correlation spectra. Binding to the polysaccharide heparin was found to induce the unfolding of preformed structural elements in OPN.A...
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12-05-2016 01:06 PM
HN-NCA heteronuclear TOCSY-NH experiment for 1 H N and 15 N sequential correlations in ( 13 C, 15 N) labelled intrinsically disordered proteins
HN-NCA heteronuclear TOCSY-NH experiment for 1 H N and 15 N sequential correlations in ( 13 C, 15 N) labelled intrinsically disordered proteins
Abstract
A simple triple resonance NMR experiment that leads to the correlation of the backbone amide resonances of each amino acid residue â??iâ?? with that of residues â??iâ??1â?? and â??i+1â?? in (13C, 15N) labelled intrinsically disordered proteins (IDPs) is presented. The experimental scheme, {HN-NCA heteronuclear TOCSY-NH}, exploits the favourable relaxation properties of IDPs and the presence of 1 ...
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08-18-2015 10:07 AM
New 13C-detected experiments for the assignment of intrinsically disordered proteins
New 13C-detected experiments for the assignment of intrinsically disordered proteins
Abstract
NMR assignment of intrinsically disordered proteins (IDPs) by conventional HN-detected methods is hampered by the small dispersion of the amide protons chemical shifts and exchange broadening of amide proton signals. Therefore several alternative assignment strategies have been proposed in the last years. Attempting to seize that dispersion of 13Câ?² and 15N chemical shifts holds even in IDPs, we recently proposed two 13C-detected experiments to directly...
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06-19-2014 10:21 PM
[NMR paper] Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Related Articles Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Chem Commun (Camb). 2013 Dec 23;
Authors: Helge Meyer N, Zangger K
Abstract
Limited spectral resolution in the proton dimension of NMR spectra is a severe problem in intrinsically disordered proteins. Here we show that homonuclear...
Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
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