ArticleScience advances2019
Solvent-dependent segmental dynamics in intrinsically disordered proteins.
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 28 papers.
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Who cites it
28 citing papers in PubMed, 68 citations in OpenAlex.
- A Bayesian Approach to Interpret Time-Resolved Experiments Using Molecular Simulations.ACS physical chemistry Au · 2026Article
- Anisosmotic Modulation of Mutant Huntingtin Aggregation vis-a-vis HSP70 Induction─Implications for Aging, Hypo-Hydration, and Neurodegeneration.ACS chemical neuroscience · 2026Article
- Measuring and locating the changes in protein structure using MELO.Nature communications · 2026Article
- Atomistic molecular dynamics simulations of intrinsically disordered proteins.Current opinion in structural biology · 2025Review
- Unraveling Hydration Shell Dynamics and Viscosity Effects Around Cyanamide Probes via 2D IR Spectroscopy.Journal of the American Chemical Society · 2025Article
- Heterogeneous Slowdown of Dynamics in the Condensate of an Intrinsically Disordered Protein.The journal of physical chemistry letters · 2024Article
- Labile assembly of a tardigrade protein induces biostasis.Protein science : a publication of the Protein Society · 2024Article
- Molecular simulations integrated with experiments for probing the interaction dynamics and binding mechanisms of intrinsically disordered proteins.Current opinion in structural biology · 2024Review
- Active learning of the thermodynamics-dynamics trade-off in protein condensates.Science advances · 2024Article
- Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.Current research in structural biology · 2024Review
- Phase Transitions of Associative Biomacromolecules.Chemical reviews · 2023Review
- Liquid-Liquid Phase Separation Modifies the Dynamic Properties of Intrinsically Disordered Proteins.Journal of the American Chemical Society · 2023Article
- Decreased Water Mobility Contributes To Increased α-Synuclein Aggregation.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- Decreased Water Mobility Contributes To Increased α-Synuclein Aggregation.Angewandte Chemie (International ed. in English) · 2023Article
- Convergent views on disordered protein dynamics from NMR and computational approaches.Biophysical journal · 2022Article
- NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.Chemical reviews · 2022Review
- Hydration Dynamics of Model Peptides with Different Hydrophobic Character.Life (Basel, Switzerland) · 2022Article
- Molecular Basis of Small-Molecule Binding to α-Synuclein.Journal of the American Chemical Society · 2022Article
- Structural and dynamic studies of the peptidase domain from Clostridium thermocellum PCAT1.Protein science : a publication of the Protein Society · 2022Article
- Machine-learning analysis of intrinsically disordered proteins identifies key factors that contribute to neurodegeneration-related aggregation.Frontiers in aging neuroscience · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein and water dynamics have a synergistic relationship, which is particularly important for intrinsically disordered proteins (IDPs), although the details of this coupling remain poorly understood. Here, we combine temperature-dependent molecular dynamics simulations using different water models with extensive nuclear magnetic resonance (NMR) relaxation to examine the importance of distinct modes of solvent and solute motion for the accurate reproduction of site-specific dynamics in IDPs. We find that water dynamics play a key role in motional processes internal to "segments" of IDPs, stretches of primary sequence that share dynamic properties and behave as discrete dynamic units. We identify a relationship between the time scales of intrasegment dynamics and the lifetime of hydrogen bonds in bulk water. Correct description of these motions is essential for accurate reproduction of protein relaxation. Our findings open important perspectives for understanding the role of hydration water on the behavior and function of IDPs in solution.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.