ArticleScience advances2019
Functional protein dynamics on uncharted time scales detected by nanoparticle-assisted NMR spin relaxation.
Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Gel-Based NMR Method for Observing Submicrosecond Protein Dynamics at Atomic Resolution.The journal of physical chemistry letters · 2026Article
- Detection of intramolecular protein dynamics on nanosecond-to-microsecond timescales by nanoparticle-assisted NMR spin relaxation (NASR).Nature protocols · 2026Review
- Kinetic Resolution of the Atomic 3D Structures Formed by Ground and Excited Conformational States in an RNA Dynamic Ensemble.Journal of the American Chemical Society · 2023Article
- Excited-state observation of active K-Ras reveals differential structural dynamics of wild-type versus oncogenic G12D and G12C mutants.Nature structural & molecular biology · 2023Article
- Intracellular environment can change protein conformational dynamics in cells through weak interactions.Science advances · 2023Article
- Synergism between x-ray crystallography and NMR residual dipolar couplings in characterizing protein dynamics.Structural dynamics (Melville, N.Y.) · 2023Article
- Binding Between Antibiotics and Polystyrene Nanoparticles Examined by NMR.ACS environmental Au · 2023Article
- Quantitative Multistate Binding Model of Silica Nanoparticle-Protein Interactions Obtained from Multinuclear Spin Relaxation.The journal of physical chemistry. B · 2022Article
- Megahertz pulse trains enable multi-hit serial femtosecond crystallography experiments at X-ray free electron lasers.Nature communications · 2022Article
- NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.Chemical reviews · 2022Review
- NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions.Progress in nuclear magnetic resonance spectroscopy · 2022Review
- A 200 nanoseconds all-atom simulation of the pH-dependent EF loop transition in bovine β-lactoglobulin. The role of the orientation of the E89 side chain.Journal of biomolecular structure & dynamics · 2022Article
- Resolving Dynamics in the Ensemble: Finding Paths through Intermediate States and Disordered Protein Structures.The journal of physical chemistry. B · 2021Article
- Quantitative Measurement of Multiprotein Nanoparticle Interactions Using NMR Spectroscopy.Analytical chemistry · 2021Article
- NMR Spin Relaxation Theory of Biomolecules Undergoing Highly Asymmetric Exchange with Large Interaction Partners.Journal of chemical theory and computation · 2021Article
- Probing driving forces for binding between nanoparticles and amino acids by saturation-transfer difference NMR.Scientific reports · 2020Article
- NMR techniques in studying water in biotechnological systems.Biophysical reviews · 2020Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein function depends critically on intrinsic internal dynamics, which is manifested in distinct ways, such as loop motions that regulate protein recognition and catalysis. Under physiological conditions, dynamic processes occur on a wide range of time scales from subpicoseconds to seconds. Commonly used NMR spin relaxation in solution provides valuable information on very fast and slow motions but is insensitive to the intermediate nanosecond to microsecond range that exceeds the protein tumbling correlation time. Presently, very little is known about the nature and functional role of these motions. It is demonstrated here how transverse spin relaxation becomes exquisitely sensitive to these motions at atomic resolution when studying proteins in the presence of nanoparticles. Application of this novel cross-disciplinary approach reveals large-scale dynamics of loops involved in functionally critical protein-protein interactions and protein-calcium ion recognition that were previously unobservable.
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