ArticleScientific reports2017
Dynamics of Hydration Water Plays a Key Role in Determining the Binding Thermodynamics of Protein Complexes.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 70 citations in OpenAlex.
- Peptides display multilayered hydration shell substructures dictated by sequence-specific surface chemistry.Nature communications · 2026Article
- Solution Phase Protein Dynamics: Influences of ESI Buffers on Hydration.Analytical chemistry · 2026Article
- Bound water as a kinetic crosslinker for bio-inspired impact-stiffening polymers.Nature communications · 2026Article
- WatCon: A Python Tool for Analysis of Conserved Water Networks Across Protein Families.JACS Au · 2025Article
- Development of DARPin T cell engagers for specific targeting of tumor-associated HLA/peptide complexes.iScience · 2025Article
- Visualize Transient Water-Mediated Hydrogen Bonds Facilitating the Formation of Enzymatic Near-Attack Conformers.JACS Au · 2025Article
- Roles of Hydration in Protein-Ligand Binding: Passive or Active Participant?The journal of physical chemistry. A · 2025Article
- Hydration (HJournal of the American Chemical Society · 2025Article
- In vivo changes in the gradient of refractive index distribution in the accommodating human lens.Experimental eye research · 2025Article
- Allostery without Conformational Change: A Native Mass Spectrometry Perspective.The journal of physical chemistry. B · 2025Article
- Binding Free Energy Analysis of Colicin D, E3 and E8 to Their Respective Cognate Immunity Proteins Using Computational Simulations.Molecules (Basel, Switzerland) · 2025Article
- Computational Approaches to Predict Protein-Protein Interactions in Crowded Cellular Environments.Chemical reviews · 2024Review
- Energetic driving force for LHCII clustering in plant membranes.Science advances · 2023Article
- Anisotropic dynamics of an interfacial enzyme active site observed using tethered substrate analogs and ultrafast 2D IR spectroscopy.The Journal of chemical physics · 2023Article
- Light, Water, and Melatonin: The Synergistic Regulation of Phase Separation in Dementia.International journal of molecular sciences · 2023Review
- Historical Silk: A Novel Method to Evaluate Degumming with Non-Invasive Infrared Spectroscopy and Spectral Deconvolution.Materials (Basel, Switzerland) · 2023Article
- Competition between chiral solvents and chiral monomers in the helical bias of supramolecular polymers.Nature chemistry · 2021Article
- Thermodynamic Origin of Differential Excipient-Lysozyme Interactions.Frontiers in molecular biosciences · 2021Article
- In silico mutagenesis of human ACE2 with S protein and translational efficiency explain SARS-CoV-2 infectivity in different species.PLoS computational biology · 2020Article
- Exploring the use of molecular dynamics in assessing protein variants for phenotypic alterations.Human mutation · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interfacial waters are considered to play a crucial role in protein-protein interactions, but in what sense and why are they important? Here, using molecular dynamics simulations and statistical thermodynamic analyses, we demonstrate distinctive dynamic characteristics of the interfacial water and investigate their implications for the binding thermodynamics. We identify the presence of extraordinarily slow (~1,000 times slower than in bulk water) hydrogen-bond rearrangements in interfacial water. We rationalize the slow rearrangements by introducing the "trapping" free energies, characterizing how strongly individual hydration waters are captured by the biomolecular surface, whose magnitude is then traced back to the number of water-protein hydrogen bonds and the strong electrostatic field produced at the binding interface. We also discuss the impact of the slow interfacial waters on the binding thermodynamics. We find that, as expected from their slow dynamics, the conventional approach to the water-mediated interaction, which assumes rapid equilibration of the waters' degrees of freedom, is inadequate. We show instead that an explicit treatment of the extremely slow interfacial waters is critical. Our results shed new light on the role of water in protein-protein interactions, highlighting the need to consider its dynamics to improve our understanding of biomolecular bindings.
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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.