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(13)C Direct Detected NMR for Challenging Systems

[Image: see text] 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 provid...

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Autores principales: Felli, Isabella C., Pierattelli, Roberta
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9136920/
https://www.ncbi.nlm.nih.gov/pubmed/35025504
http://dx.doi.org/10.1021/acs.chemrev.1c00871
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author Felli, Isabella C.
Pierattelli, Roberta
author_facet Felli, Isabella C.
Pierattelli, Roberta
author_sort Felli, Isabella C.
collection PubMed
description [Image: see text] 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 the structural and dynamic characterization of a protein in isolation, as part of a larger complex, or even inside a living cell. We present the different properties of (13)C with respect to (1)H, which provide the rationale for the experiments developed and their application, the technical aspects that need to be faced, and the many experimental variants designed to address different cases. Application areas where these experiments successfully complement proton NMR are also described.
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spelling pubmed-91369202022-05-28 (13)C Direct Detected NMR for Challenging Systems Felli, Isabella C. Pierattelli, Roberta Chem Rev [Image: see text] 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 the structural and dynamic characterization of a protein in isolation, as part of a larger complex, or even inside a living cell. We present the different properties of (13)C with respect to (1)H, which provide the rationale for the experiments developed and their application, the technical aspects that need to be faced, and the many experimental variants designed to address different cases. Application areas where these experiments successfully complement proton NMR are also described. American Chemical Society 2022-01-13 2022-05-25 /pmc/articles/PMC9136920/ /pubmed/35025504 http://dx.doi.org/10.1021/acs.chemrev.1c00871 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Felli, Isabella C.
Pierattelli, Roberta
(13)C Direct Detected NMR for Challenging Systems
title (13)C Direct Detected NMR for Challenging Systems
title_full (13)C Direct Detected NMR for Challenging Systems
title_fullStr (13)C Direct Detected NMR for Challenging Systems
title_full_unstemmed (13)C Direct Detected NMR for Challenging Systems
title_short (13)C Direct Detected NMR for Challenging Systems
title_sort (13)c direct detected nmr for challenging systems
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9136920/
https://www.ncbi.nlm.nih.gov/pubmed/35025504
http://dx.doi.org/10.1021/acs.chemrev.1c00871
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