Thanks to recent improvements in NMR spectrometer hardware and pulse sequence design, modern ^(13)C NMR has become a useful tool for biomolecular applications. The complete assignment of a protein can be accomplished by using ^(13)C detected multinuclear experiments and it can provide unique information relevant for the study of a variety of different biomolecules including paramagnetic proteins and intrinsically disordered proteins. A wide range of NMR observables can be measured, concurring to...
[NMR paper] Methyl TROSY spectroscopy: A versatile NMR approach to study challenging biological systems.
Methyl TROSY spectroscopy: A versatile NMR approach to study challenging biological systems.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Methyl TROSY spectroscopy: A versatile NMR approach to study challenging biological systems.
Prog Nucl Magn Reson Spectrosc. 2020 Feb;116:56-84
Authors: Schütz S, Sprangers R
Abstract
A major goal in structural biology is to unravel how molecular machines function in detail. To that end,...
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03-07-2020 06:20 PM
Direct 13 C-detected NMR experiments for mapping and characterization of hydrogen bonds in RNA
Direct 13 C-detected NMR experiments for mapping and characterization of hydrogen bonds in RNA
Abstract
In RNA secondary structure determination, it is essential to determine whether a nucleotide is base-paired and not. Base-pairing of nucleotides is mediated by hydrogen bonds. The NMR characterization of hydrogen bonds relies on experiments correlating the NMR resonances of exchangeable protons and can be best performed for structured parts of the RNA, where labile hydrogen atoms are protected from solvent exchange. Functionally important regions in...
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02-06-2016 03:10 PM
[NMR paper] Longitudinal relaxation properties of (1)H(N) and (1)H(?) determined by direct-detected (13)C NMR experiments to study intrinsically disordered proteins (IDPs).
Longitudinal relaxation properties of (1)H(N) and (1)H(?) determined by direct-detected (13)C NMR experiments to study intrinsically disordered proteins (IDPs).
Longitudinal relaxation properties of (1)H(N) and (1)H(?) determined by direct-detected (13)C NMR experiments to study intrinsically disordered proteins (IDPs).
J Magn Reson. 2015 Feb 12;254:19-26
Authors: Hošek T, Gil-Caballero S, Pierattelli R, Brutscher B, Felli IC
Abstract
Intrinsically disordered proteins (IDPs) are functional proteins containing large...
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03-17-2015 05:12 PM
Longitudinal relaxation properties of 1HN and 1H? determined by direct-detected 13C NMR experiments to study intrinsically disordered proteins (IDPs)
Longitudinal relaxation properties of 1HN and 1H? determined by direct-detected 13C NMR experiments to study intrinsically disordered proteins (IDPs)
Publication date: Available online 12 February 2015
Source:Journal of Magnetic Resonance</br>
Author(s): Tomáš Hošek , Sergi Gil-Caballero , Roberta Pierattelli , Bernhard Brutscher , Isabella C. Felli</br>
Intrinsically disordered proteins (IDPs) are functional proteins containing large fragments characterized by high local mobility. Bioinformatic studies have suggested that a significant fraction (more than 30%)...
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02-12-2015 07:48 PM
High-field ELDOR-detected NMR study of a nitroxide radical in disordered solids:Towards characterization of heterogeneity of microenvironments in spin-labeled systems
High-field ELDOR-detected NMR study of a nitroxide radical in disordered solids:Towards characterization of heterogeneity of microenvironments in spin-labeled systems
Publication date: Available online 12 March 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Anna Nalepa , Klaus Möbius , Wolfgang Lubitz , Anton Savitsky</br>
The combination of high-field EPR with site-directed spin-labeling (SDSL) techniques employing nitroxide radicals has turned out to be particularly powerful in probing the polarity and proticity characteristics of protein/matrix...
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03-12-2014 01:35 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...
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11-11-2013 01:30 AM
[NMR paper] Proton-Detected Solid-State NMR Spectroscopy at Aliphatic Sites: Application to Crystalline Systems.
Proton-Detected Solid-State NMR Spectroscopy at Aliphatic Sites: Application to Crystalline Systems.
Related Articles Proton-Detected Solid-State NMR Spectroscopy at Aliphatic Sites: Application to Crystalline Systems.
Acc Chem Res. 2013 Jun 7;
Authors: Asami S, Reif B
Abstract
When applied to biomolecules, solid-state NMR suffers from low sensitivity and resolution. The major obstacle to applying proton detection in the solid state is the proton dipolar network, and deuteration can help avoid this problem. In the past, researchers...
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06-12-2013 11:42 AM
13C-direct detected NMR experiments for the sequential J-based resonance assignment o
Abstract We present here a set of 13C-direct detected NMR experiments to facilitate the resonance assignment of RNA oligonucleotides. Three experiments have been developed: (1) the (H)CC-TOCSY-experiment utilizing a virtual decoupling scheme to assign the intraresidual ribose 13C-spins, (2) the (H)CPC-experiment that correlates each phosphorus with the C4â?² nuclei of adjacent nucleotides via J(C,P) couplings and (3) the (H)CPC-CCH-TOCSY-experiment that correlates the phosphorus nuclei with the respective C1â?²,H1â?² ribose signals. The experiments were applied to two RNA hairpin structures....