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NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins

[Image: see text] Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing essential roles in all aspects of cellular and extracellular biochemistry. To understand their function, it is necessary to determine their structural and dynamic behavior and to describe the p...

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Autores principales: Camacho-Zarco, Aldo R., Schnapka, Vincent, Guseva, Serafima, Abyzov, Anton, Adamski, Wiktor, Milles, Sigrid, Jensen, Malene Ringkjøbing, Zidek, Lukas, Salvi, Nicola, Blackledge, Martin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9136928/
https://www.ncbi.nlm.nih.gov/pubmed/35446534
http://dx.doi.org/10.1021/acs.chemrev.1c01023
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author Camacho-Zarco, Aldo R.
Schnapka, Vincent
Guseva, Serafima
Abyzov, Anton
Adamski, Wiktor
Milles, Sigrid
Jensen, Malene Ringkjøbing
Zidek, Lukas
Salvi, Nicola
Blackledge, Martin
author_facet Camacho-Zarco, Aldo R.
Schnapka, Vincent
Guseva, Serafima
Abyzov, Anton
Adamski, Wiktor
Milles, Sigrid
Jensen, Malene Ringkjøbing
Zidek, Lukas
Salvi, Nicola
Blackledge, Martin
author_sort Camacho-Zarco, Aldo R.
collection PubMed
description [Image: see text] Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing essential roles in all aspects of cellular and extracellular biochemistry. To understand their function, it is necessary to determine their structural and dynamic behavior and to describe the physical chemistry of their interaction trajectories. Nuclear magnetic resonance is perfectly adapted to this task, providing ensemble averaged structural and dynamic parameters that report on each assigned resonance in the molecule, unveiling otherwise inaccessible insight into the reaction kinetics and thermodynamics that are essential for function. In this review, we describe recent applications of NMR-based approaches to understanding the conformational energy landscape, the nature and time scales of local and long-range dynamics and how they depend on the environment, even in the cell. Finally, we illustrate the ability of NMR to uncover the mechanistic basis of functional disordered molecular assemblies that are important for human health.
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spelling pubmed-91369282022-05-28 NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins Camacho-Zarco, Aldo R. Schnapka, Vincent Guseva, Serafima Abyzov, Anton Adamski, Wiktor Milles, Sigrid Jensen, Malene Ringkjøbing Zidek, Lukas Salvi, Nicola Blackledge, Martin Chem Rev [Image: see text] Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing essential roles in all aspects of cellular and extracellular biochemistry. To understand their function, it is necessary to determine their structural and dynamic behavior and to describe the physical chemistry of their interaction trajectories. Nuclear magnetic resonance is perfectly adapted to this task, providing ensemble averaged structural and dynamic parameters that report on each assigned resonance in the molecule, unveiling otherwise inaccessible insight into the reaction kinetics and thermodynamics that are essential for function. In this review, we describe recent applications of NMR-based approaches to understanding the conformational energy landscape, the nature and time scales of local and long-range dynamics and how they depend on the environment, even in the cell. Finally, we illustrate the ability of NMR to uncover the mechanistic basis of functional disordered molecular assemblies that are important for human health. American Chemical Society 2022-04-21 2022-05-25 /pmc/articles/PMC9136928/ /pubmed/35446534 http://dx.doi.org/10.1021/acs.chemrev.1c01023 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 Camacho-Zarco, Aldo R.
Schnapka, Vincent
Guseva, Serafima
Abyzov, Anton
Adamski, Wiktor
Milles, Sigrid
Jensen, Malene Ringkjøbing
Zidek, Lukas
Salvi, Nicola
Blackledge, Martin
NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
title NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
title_full NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
title_fullStr NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
title_full_unstemmed NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
title_short NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
title_sort nmr provides unique insight into the functional dynamics and interactions of intrinsically disordered proteins
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9136928/
https://www.ncbi.nlm.nih.gov/pubmed/35446534
http://dx.doi.org/10.1021/acs.chemrev.1c01023
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