ArticleProtein science : a publication of the Protein Society2014
Solution properties of γ-crystallins: hydration of fish and mammal 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 17 papers.
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Who cites it
17 citing papers in PubMed, 35 citations in OpenAlex.
- In the Beginning: Let Hydration Be Coded in Proteins for Manifestation and Modulation by Salts and Adenosine Triphosphate.International journal of molecular sciences · 2024Review
- Review
- Transcriptomic evidence for visual adaptation during the aquatic to terrestrial metamorphosis in leopard frogs.BMC biology · 2022Article
- Acquired Disorder and Asymmetry in a Domain-Swapped Model for γ-Crystallin Aggregation.Journal of molecular biology · 2022Article
- Adenosine triphosphate energy-independently controls protein homeostasis with unique structure and diverse mechanisms.Protein science : a publication of the Protein Society · 2021Review
- Genetic Adaptations in Mudskipper and Tetrapod Give Insights into Their Convergent Water-to-Land Transition.Animals : an open access journal from MDPI · 2021Article
- Function and Aggregation in Structural Eye Lens Crystallins.Accounts of chemical research · 2020Review
- Ultrafast Dynamics of Water-Protein Coupled Motions around the Surface of Eye Crystallin.Journal of the American Chemical Society · 2020Article
- Measuring Ultra-Weak Protein Self-Association by Non-ideal Sedimentation Velocity.Journal of the American Chemical Society · 2019Article
- Protein refractive index increment is determined by conformation as well as composition.Journal of physics. Condensed matter : an Institute of Physics journal · 2018Article
- 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
- In Vivo Brillouin Analysis of the Aging Crystalline Lens.Investigative ophthalmology & visual science · 2016Article
- Stability of Protein-Specific Hydration Shell on Crowding.Journal of the American Chemical Society · 2016Article
- Measurement of the temperature of the resting rotor in analytical ultracentrifugation.Analytical biochemistry · 2014Article
- Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells.Progress in biophysics and molecular biology · 2014Review
- The βγ-crystallins: native state stability and pathways to aggregation.Progress in biophysics and molecular biology · 2014Review
- Solution properties of γ-crystallins: compact structure and low frictional ratio are conserved properties of diverse γ-crystallins.Protein science : a publication of the Protein Society · 2014Article
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Authors and funding
6 authors at 4 institutions in 1 country.
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Abstract
Lens γ crystallins are found at the highest protein concentration of any tissue, ranging from 300 mg/mL in some mammals to over 1000 mg/mL in fish. Such high concentrations are necessary for the refraction of light, but impose extreme requirements for protein stability and solubility. γ-crystallins, small stable monomeric proteins, are particularly associated with the lowest hydration regions of the lens. Here, we examine the solvation of selected γ-crystallins from mammals (human γD and mouse γS) and fish (zebrafish γM2b and γM7). The thermodynamic water binding coefficient B₁ could be probed by sucrose expulsion, and the hydrodynamic hydration shell of tightly bound water was probed by translational diffusion and structure-based hydrodynamic boundary element modeling. While the amount of tightly bound water of human γD was consistent with that of average proteins, the water binding of mouse γS was found to be relatively low. γM2b and γM7 crystallins were found to exhibit extremely low degrees hydration, consistent with their role in the fish lens. γM crystallins have a very high methionine content, in some species up to 15%. Structure-based modeling of hydration in γM7 crystallin suggests low hydration is associated with the large number of surface methionine residues, likely in adaptation to the extremely high concentration and low hydration environment in fish lenses. Overall, the degree of hydration appears to balance stability and tissue density requirements required to produce and maintain the optical properties of the lens in different vertebrate species.
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