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@article{1860349, author = {CamachoandZarco, Aldo R. and Schnapka, Vincent and Guseva, Serafima and Abyzov, Anton and Adamski, Wiktor and Milles, Sigrid and Jensen, Malene Ringkjøbing and Žídek, Lukáš and Salvi, Nicola and Blackledge, Martin}, article_location = {UNITED STATES}, article_number = {10}, doi = {http://dx.doi.org/10.1021/acs.chemrev.1c01023}, keywords = {Dynamics; Physical chemistry; Proteins; Reaction kinetics; Thermodynamics}, language = {eng}, issn = {0009-2665}, journal = {CHEMICAL REVIEWS}, title = {NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins}, url = {https://pubs.acs.org/doi/10.1021/acs.chemrev.1c01023}, volume = {122}, year = {2022} }
TY - JOUR ID - 1860349 AU - Camacho-Zarco, Aldo R. - Schnapka, Vincent - Guseva, Serafima - Abyzov, Anton - Adamski, Wiktor - Milles, Sigrid - Jensen, Malene Ringkjøbing - Žídek, Lukáš - Salvi, Nicola - Blackledge, Martin PY - 2022 TI - NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins JF - CHEMICAL REVIEWS VL - 122 IS - 10 SP - 9331-9356 EP - 9331-9356 PB - AMER CHEMICAL SOC SN - 00092665 KW - Dynamics KW - Physical chemistry KW - Proteins KW - Reaction kinetics KW - Thermodynamics UR - https://pubs.acs.org/doi/10.1021/acs.chemrev.1c01023 N2 - 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. ER -
CAMACHO-ZARCO, Aldo R., Vincent SCHNAPKA, Serafima GUSEVA, Anton ABYZOV, Wiktor ADAMSKI, Sigrid MILLES, Malene Ringkjøbing JENSEN, Lukáš ŽÍDEK, Nicola SALVI a Martin BLACKLEDGE. NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins. \textit{CHEMICAL REVIEWS}. UNITED STATES: AMER CHEMICAL SOC, 2022, roč.~122, č.~10, s.~9331-9356. ISSN~0009-2665. Dostupné z: https://dx.doi.org/10.1021/acs.chemrev.1c01023.
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