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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,...

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Detalles Bibliográficos
Autores principales: Felli, Isabella C., Bermel, Wolfgang, Pierattelli, Roberta
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Copernicus GmbH 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10539766/
https://www.ncbi.nlm.nih.gov/pubmed/37904768
http://dx.doi.org/10.5194/mr-2-511-2021
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author Felli, Isabella C.
Bermel, Wolfgang
Pierattelli, Roberta
author_facet Felli, Isabella C.
Bermel, Wolfgang
Pierattelli, Roberta
author_sort Felli, Isabella C.
collection PubMed
description 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 protons in proline residues within polypeptide chains. The novel experiments have very interesting properties for the investigations of IDPs/IDRs of increasing complexity.
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spelling pubmed-105397662023-10-30 Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues Felli, Isabella C. Bermel, Wolfgang Pierattelli, Roberta Magn Reson (Gott) Research Article 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 protons in proline residues within polypeptide chains. The novel experiments have very interesting properties for the investigations of IDPs/IDRs of increasing complexity. Copernicus GmbH 2021-07-01 /pmc/articles/PMC10539766/ /pubmed/37904768 http://dx.doi.org/10.5194/mr-2-511-2021 Text en Copyright: © 2021 Isabella C. Felli et al. https://creativecommons.org/licenses/by/4.0/This work is licensed under the Creative Commons Attribution 4.0 International License. To view a copy of this licence, visit https://creativecommons.org/licenses/by/4.0/
spellingShingle Research Article
Felli, Isabella C.
Bermel, Wolfgang
Pierattelli, Roberta
Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
title Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
title_full Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
title_fullStr Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
title_full_unstemmed Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
title_short Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
title_sort exclusively heteronuclear nmr experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10539766/
https://www.ncbi.nlm.nih.gov/pubmed/37904768
http://dx.doi.org/10.5194/mr-2-511-2021
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