ArticleProceedings of the National Academy of Sciences of the United States of America2014
Hard sphere-like glass transition in eye lens α-crystallin solutions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- A Peptide-Based Strategy to Disrupt Oxidation-Induced Aggregation of γC-Crystallin Missense Mutant.JACS Au · 2026Article
- Lipoprotein diffusion in dense yolk plasma is governed by softness, hydrodynamics, and caging: Insights from MHz-XPCS.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Testing mixing rules for structural and dynamical quantities in multi-component crowded protein solutions.APL bioengineering · 2024Article
- Combining Scattering Experiments and Colloid Theory to Characterize Charge Effects in Concentrated Antibody Solutions.Molecular pharmaceutics · 2024Article
- High-pressure X-ray photon correlation spectroscopy at fourth-generation synchrotron sources.Journal of synchrotron radiation · 2024Article
- Design and Characterization of Model Systems that Promote and Disrupt Transparency of Vertebrate Crystallins In Vitro.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Phase-Decorrelation Optical Coherence Tomography Measurement of Cold-Induced Nuclear Cataract.Translational vision science & technology · 2023Article
- Molecular rotors in haemoglobin and bovine serum albumin proteins.Journal of the Royal Society, Interface · 2022Article
- Droplet-Based Microfluidic Tool to Quantify Viscosity of Concentrating Protein Solutions.Pharmaceutical research · 2021Article
- Crowding in the Eye Lens: Modeling the Multisubunit Protein β-Crystallin with a Colloidal Approach.Biophysical journal · 2020Article
- Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.International journal of molecular sciences · 2020Review
- Eye lens crystallin proteins inhibit the autocatalytic amyloid amplification nature of mature α-synuclein fibrils.PloS one · 2020Article
- Evolutionary drivers of protein shape.Scientific reports · 2019Article
- Concentration Effects in the Interaction of Monoclonal Antibodies (mAbs) with their Immediate Environment Characterized by EPR Spectroscopy.Molecules (Basel, Switzerland) · 2019Article
- Weak Shape Anisotropy Leads to a Nonmonotonic Contribution to Crowding, Impacting Protein Dynamics under Physiologically Relevant Conditions.The journal of physical chemistry. B · 2018Article
- Universal glass-forming behavior of in vitro and living cytoplasm.Scientific reports · 2017Article
- Comparative Study of the Collective Dynamics of Proteins and Inorganic Nanoparticles.Scientific reports · 2017Article
- Statistical-thermodynamic model for light scattering from eye lens protein mixtures.The Journal of chemical physics · 2017Article
- Dramatic influence of patchy attractions on short-time protein diffusion under crowded conditions.Science advances · 2016Article
- Unusual dynamics of concentration fluctuations in solutions of weakly attractive globular proteins.The journal of physical chemistry letters · 2015Article
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Authors and funding
7 authors.
Funding
Abstract
We study the equilibrium liquid structure and dynamics of dilute and concentrated bovine eye lens α-crystallin solutions, using small-angle X-ray scattering, static and dynamic light scattering, viscometry, molecular dynamics simulations, and mode-coupling theory. We find that a polydisperse Percus-Yevick hard-sphere liquid-structure model accurately reproduces both static light scattering data and small-angle X-ray scattering liquid structure data from α-crystallin solutions over an extended range of protein concentrations up to 290 mg/mL or 49% vol fraction and up to ca. 330 mg/mL for static light scattering. The measured dynamic light scattering and viscosity properties are also consistent with those of hard-sphere colloids and show power laws characteristic of an approach toward a glass transition at α-crystallin volume fractions near 58%. Dynamic light scattering at a volume fraction beyond the glass transition indicates formation of an arrested state. We further perform event-driven molecular dynamics simulations of polydisperse hard-sphere systems and use mode-coupling theory to compare the measured dynamic power laws with those of hard-sphere models. The static and dynamic data, simulations, and analysis show that aqueous eye lens α-crystallin solutions exhibit a glass transition at high concentrations that is similar to those found in hard-sphere colloidal systems. The α-crystallin glass transition could have implications for the molecular basis of presbyopia and the kinetics of molecular change during cataractogenesis.
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