[NMR paper] Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
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...
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] Triple resonance [Formula: see text] NMR relaxation experiments for studies of intrinsically disordered proteins.
Triple resonance NMR relaxation experiments for studies of intrinsically disordered proteins.
Related Articles Triple resonance NMR relaxation experiments for studies of intrinsically disordered proteins.
J Biomol NMR. 2017 Oct 25;:
Authors: Srb P, Nová?ek J, Kade?ávek P, Rabatinová A, Krásný L, Žídková J, Bobálová J, Sklená? V, Žídek L
Abstract
Description of protein dynamics is known to be essential in understanding their function. Studies based on a well established NMR relaxation methodology have been applied to a large...
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10-28-2017 08:03 AM
Triple resonance $$^{15}\hbox {N}$$ 15 N NMR relaxation experiments for studies of intrinsically disordered proteins
Triple resonance $$^{15}\hbox {N}$$ 15 N NMR relaxation experiments for studies of intrinsically disordered proteins
Abstract
Description of protein dynamics is known to be essential in understanding their function. Studies based on a well established \(^{15}\hbox {N}\) NMR relaxation methodology have been applied to a large number of systems....
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10-25-2017 10:14 PM
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] High-dimensionality (13)C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.
High-dimensionality (13)C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.
Related Articles High-dimensionality (13)C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.
J Biomol NMR. 2013 Nov 8;
Authors: Bermel W, Felli IC, Gonnelli L, Ko?mi?ski W, Piai A, Pierattelli R, Zawadzka-Kazimierczuk A
Abstract
We present three novel exclusively heteronuclear 5D (13)C direct-detected NMR experiments, namely (H(N-flip)N)CONCACON, (HCA)CONCACON and...
Troubleshooting Guide to Expressing Intrinsically Disordered Proteins for Use in NMR Experiments - Frontiers
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