How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?
| Autor: | Nicolas Bolik-Coulon, Matthias Ernst, Fabien Ferrage, Albert A. Smith, Beat H. Meier |
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| Přispěvatelé: | Universität Leipzig [Leipzig], Laboratoire des biomolécules (LBM UMR 7203), Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Département de Chimie - ENS Paris, École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Chimie Moléculaire de Paris Centre (FR 2769), Institut de Chimie du CNRS (INC)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich) |
| Rok vydání: | 2021 |
| Předmět: |
Relaxometry
010402 general chemistry 01 natural sciences Biochemistry Article [CHIM]Chemical Sciences Isoleucine Nuclear Magnetic Resonance Biomolecular Spectroscopy Detector analysis Ubiquitin 010405 organic chemistry Chemistry Protein dynamics Resolution (electron density) Relaxation (NMR) Dynamics (mechanics) Detector Proteins Rotational diffusion Nanosecond Dynamics 0104 chemical sciences Solutions Chemical physics Solution-state NMR |
| Zdroj: | Journal of Biomolecular NMR Journal of Biomolecular NMR, 75 (2-3) Journal of Biomolecular NMR, Springer Verlag, 2021, ⟨10.1007/s10858-021-00361-1⟩ Journal of Biomolecular Nmr |
| ISSN: | 1573-5001 0925-2738 |
| DOI: | 10.1007/s10858-021-00361-1 |
| Popis: | The dynamics of molecules in solution is usually quantified by the determination of timescale-specific amplitudes of motions. High-resolution nuclear magnetic resonance (NMR) relaxometry experiments—where the sample is transferred to low fields for longitudinal (T1) relaxation, and back to high field for detection with residue-specific resolution—seeks to increase the ability to distinguish the contributions from motion on timescales slower than a few nanoseconds. However, tumbling of a molecule in solution masks some of these motions. Therefore, we investigate to what extent relaxometry improves timescale resolution, using the “detector” analysis of dynamics. Here, we demonstrate improvements in the characterization of internal dynamics of methyl-bearing side chains by carbon-13 relaxometry in the small protein ubiquitin. We show that relaxometry data leads to better information about nanosecond motions as compared to high-field relaxation data only. Our calculations show that gains from relaxometry are greater with increasing correlation time of rotational diffusion. Journal of Biomolecular NMR, 75 (2-3) ISSN:0925-2738 ISSN:1573-5001 |
| Databáze: | OpenAIRE |
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