ArticleProtein science : a publication of the Protein Society2014
Solution properties of γ-crystallins: compact structure and low frictional ratio are conserved properties of diverse γ-crystallins.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Human Crystallin Variation and Cataract.Investigative ophthalmology & visual science · 2026Review
- Comparative analysis of the structure and crystallin composition of the lenses of freshwater fish and gastropods with respect to their vision.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2025Article
- Age-Dependent Changes in the Water Content and Optical Power of the In Vivo Mouse Lens Revealed by Multi-Parametric MRI and Optical Modeling.Investigative ophthalmology & visual science · 2023Article
- Acquired Disorder and Asymmetry in a Domain-Swapped Model for γ-Crystallin Aggregation.Journal of molecular biology · 2022Article
- Synonymous mutations in the phosphoglycerate kinase 1 gene induce an altered response to protein misfolding inFrontiers in microbiology · 2022Article
- Redox chemistry of lens crystallins: A system of cysteines.Experimental eye research · 2021Review
- MALDI imaging mass spectrometry of β- and γ-crystallins in the ocular lens.Journal of mass spectrometry : JMS · 2020Article
- Ultrafast Dynamics of Water-Protein Coupled Motions around the Surface of Eye Crystallin.Journal of the American Chemical Society · 2020Article
- Divalent Cations and the Divergence ofBiochemistry · 2019Article
- Measuring Ultra-Weak Protein Self-Association by Non-ideal Sedimentation Velocity.Journal of the American Chemical Society · 2019Article
- Crystal Structure of Chicken γS-Crystallin Reveals Lattice Contacts with Implications for Function in the Lens and the Evolution of the βγ-Crystallins.Structure (London, England : 1993) · 2017Article
- γS-crystallin proteins from the Antarctic nototheniid toothfish: a model system for investigating differential resistance to chemical and thermal denaturation.The journal of physical chemistry. B · 2014Article
- Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells.Progress in biophysics and molecular biology · 2014Review
- Solution properties of γ-crystallins: hydration of fish and mammal γ-crystallins.Protein science : a publication of the Protein Society · 2014Article
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4 authors at 3 institutions in 1 country.
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Abstract
γ-crystallins are highly specialized proteins of the vertebrate eye lens where they survive without turnover under high molecular crowding while maintaining transparency. They share a tightly folded structural template but there are striking differences among species. Their amino acid compositions are unusual. Even in mammals, γ-crystallins have high contents of sulfur-containing methionine and cysteine, but this reaches extremes in fish γM-crystallins with up to 15% Met. In addition, fish γM-crystallins do not conserve the paired tryptophan residues found in each domain in mammalian γ-crystallins and in the related β-crystallins. To gain insight into important, evolutionarily conserved properties and functionality of γ-crystallins, zebrafish (Danio rerio) γM2b and γM7 were compared with mouse γS and human γD. For all four proteins, far UV CD spectra showed the expected β-sheet secondary structure. Like the mammalian proteins, γM7 was highly soluble but γM2b was much less so. The heat and denaturant stability of both fish proteins was lower than either mammalian protein. The ability of full-length and truncated versions of human αB-crystallin to retard aggregation of the heat denatured proteins also showed differences. However, when solution behavior was investigated by sedimentation velocity experiments, the diverse γ-crystallins showed remarkably similar hydrodynamic properties with low frictional ratios and partial specific volumes. The solution behavior of γ-crystallins, with highly compact structures suited for the densely packed environment of the lens, seems to be highly conserved and appears largely independent of amino acid composition.
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