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Molecular conformations and dynamics in the extracellular matrix of mammalian structural tissues: Solid-state NMR spectroscopy approaches

Solid-state NMR spectroscopy has played an important role in multidisciplinary studies of the extracellular matrix. Here we review how solid-state NMR has been used to probe collagen molecular conformations, dynamics, post-translational modifications and non-enzymatic chemical changes, and in calcif...

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Autores principales: Murgoci, Adrian, Duer, Melinda
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8551230/
https://www.ncbi.nlm.nih.gov/pubmed/34746737
http://dx.doi.org/10.1016/j.mbplus.2021.100086
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author Murgoci, Adrian
Duer, Melinda
author_facet Murgoci, Adrian
Duer, Melinda
author_sort Murgoci, Adrian
collection PubMed
description Solid-state NMR spectroscopy has played an important role in multidisciplinary studies of the extracellular matrix. Here we review how solid-state NMR has been used to probe collagen molecular conformations, dynamics, post-translational modifications and non-enzymatic chemical changes, and in calcified tissues, the molecular structure of bone mineral and its interface with collagen. We conclude that NMR spectroscopy can deliver vital information that in combination with data from structural imaging techniques, can result in significant new insight into how the extracellular matrix plays its multiple roles.
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spelling pubmed-85512302021-11-04 Molecular conformations and dynamics in the extracellular matrix of mammalian structural tissues: Solid-state NMR spectroscopy approaches Murgoci, Adrian Duer, Melinda Matrix Biol Plus Special Section on Molecular and Supramolecular structure of the extracellular matrix; Edited by Sylvie Ricard-Blum. Solid-state NMR spectroscopy has played an important role in multidisciplinary studies of the extracellular matrix. Here we review how solid-state NMR has been used to probe collagen molecular conformations, dynamics, post-translational modifications and non-enzymatic chemical changes, and in calcified tissues, the molecular structure of bone mineral and its interface with collagen. We conclude that NMR spectroscopy can deliver vital information that in combination with data from structural imaging techniques, can result in significant new insight into how the extracellular matrix plays its multiple roles. Elsevier 2021-10-06 /pmc/articles/PMC8551230/ /pubmed/34746737 http://dx.doi.org/10.1016/j.mbplus.2021.100086 Text en © 2021 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Special Section on Molecular and Supramolecular structure of the extracellular matrix; Edited by Sylvie Ricard-Blum.
Murgoci, Adrian
Duer, Melinda
Molecular conformations and dynamics in the extracellular matrix of mammalian structural tissues: Solid-state NMR spectroscopy approaches
title Molecular conformations and dynamics in the extracellular matrix of mammalian structural tissues: Solid-state NMR spectroscopy approaches
title_full Molecular conformations and dynamics in the extracellular matrix of mammalian structural tissues: Solid-state NMR spectroscopy approaches
title_fullStr Molecular conformations and dynamics in the extracellular matrix of mammalian structural tissues: Solid-state NMR spectroscopy approaches
title_full_unstemmed Molecular conformations and dynamics in the extracellular matrix of mammalian structural tissues: Solid-state NMR spectroscopy approaches
title_short Molecular conformations and dynamics in the extracellular matrix of mammalian structural tissues: Solid-state NMR spectroscopy approaches
title_sort molecular conformations and dynamics in the extracellular matrix of mammalian structural tissues: solid-state nmr spectroscopy approaches
topic Special Section on Molecular and Supramolecular structure of the extracellular matrix; Edited by Sylvie Ricard-Blum.
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8551230/
https://www.ncbi.nlm.nih.gov/pubmed/34746737
http://dx.doi.org/10.1016/j.mbplus.2021.100086
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