ArticleJournal of the American Chemical Society2011
Role of hydration force in the self-assembly of collagens and amyloid steric zipper filaments.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed.
- Water and Collagen: A Mystery Yet to Unfold.Biomacromolecules · 2025Review
- CHARMM at 45: Enhancements in Accessibility, Functionality, and Speed.The journal of physical chemistry. B · 2024Review
- Heterogeneous and Allosteric Role of Surface Hydration for Protein-Ligand Binding.Journal of chemical theory and computation · 2023Article
- Article
- Contrasting Local and Macroscopic Effects of Collagen Hydroxylation.International journal of molecular sciences · 2021Article
- Effect of Methylation on Local Mechanics and Hydration Structure of DNA.Biophysical journal · 2018Article
- Ultrafast Time-Resolved Studies on Fluorescein for Recognition Strands Architecture in Amyloid Fibrils.The journal of physical chemistry. B · 2018Article
- Article
- Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils.Biophysical journal · 2017Article
- Article
- Chain registry and load-dependent conformational dynamics of collagen.Biomacromolecules · 2014Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
In protein self-assembly, types of surfaces determine the force between them. Yet the extent to which the surrounding water contributes to this force remains as a fundamental question. Here we study three self-assembling filament systems that respectively have hydrated (collagen), dry nonpolar, and dry polar (amyloid) interfaces. Using molecular dynamics simulations, we calculate and compare local hydration maps and hydration forces. We find that the primary hydration shells are formed all over the surface, regardless of the types of the underlying amino acids. The weakly oscillating hydration force arises from coalescence and depletion of hydration shells as two filaments approach, whereas local water diffusion, orientation, or hydrogen-bonding events have no direct effect. Hydration forces between hydrated, polar, and nonpolar interfaces differ in the amplitude and phase of the oscillation relative to the equilibrium surface separation. Therefore, water-mediated interactions between these protein surfaces, ranging in character from "hydrophobic" to "hydrophilic", have a common molecular origin based on the robustly formed hydration shells, which is likely applicable to a broad range of biomolecular assemblies whose interfacial geometry is similar in length scale to those of the present study.
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Registered trials
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