A Unified Description of Intrinsically Disordered Protein Dynamics under Physiological Conditions Using NMR Spectroscopy
| Autor: | Anton Abyzov, Christophe Moreau, Nicola Salvi, Martin Blackledge, Wiktor Adamski, Malene Ringkjøbing Jensen, Justine Magnat, Damien Maurin, Sigrid Milles |
|---|---|
| Přispěvatelé: | Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017) |
| Rok vydání: | 2019 |
| Předmět: |
MAP Kinase Kinase 4
Protein Conformation 010402 general chemistry Intrinsically disordered proteins 01 natural sciences Biochemistry Sendai virus Catalysis Viral Proteins Xenopus laevis Colloid and Surface Chemistry Protein structure Protein Domains Animals Spectroscopy Nuclear Magnetic Resonance Biomolecular chemistry.chemical_classification [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Nitrogen Isotopes Biomolecule Protein dynamics Relaxation (NMR) General Chemistry Nuclear magnetic resonance spectroscopy 0104 chemical sciences Intrinsically Disordered Proteins Range (mathematics) Nucleoproteins chemistry Chemical physics Oocytes |
| Zdroj: | Journal of the American Chemical Society Journal of the American Chemical Society, American Chemical Society, 2019, 141 (44), pp.17817-17829. ⟨10.1021/jacs.9b09002⟩ Journal of the American Chemical Society, 2019, 141 (44), pp.17817-17829. ⟨10.1021/jacs.9b09002⟩ |
| ISSN: | 1520-5126 0002-7863 |
| Popis: | International audience; Intrinsically disordered proteins (IDPs) are flexible biomolecules whose essential functions are defined by their dynamic nature. Nuclear magnetic resonance (NMR) spectroscopy is ideally suited to the investigation of this behavior at atomic resolution. NMR relaxation is increasingly used to detect conformational dynamics in free and bound forms of IDPs under conditions approaching physiological, although a general framework providing a quantitative interpretation of these exquisitely sensitive probes as a function of experimental conditions is still lacking. Here, measuring an extensive set of relaxation rates sampling multiple-time-scale dynamics over a broad range of crowding conditions, we develop and test an integrated analytical description that accurately portrays the motion of IDPs as a function of the intrinsic properties of the crowded molecular environment. In particular we observe a strong dependence of both short-range and long-range motional time scales of the protein on the friction of the solvent. This tight coupling between the dynamic behavior of the IDP and its environment allows us to develop analytical expressions for protein motions and NMR relaxation properties that can be accurately applied over a vast range of experimental conditions. This unified dynamic description provides new insight into the physical behavior of IDPs, extending our ability to quantitatively investigate their conformational dynamics under complex environmental conditions, and accurately predicting relaxation rates reporting on motions on time scales up to tens of nanoseconds, both in vitro and in cellulo. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|