ArticlePhysical biology2011
The role of macromolecular crowding in the evolution of lens crystallins with high molecular refractive index.
Article in Physical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 35 citations in OpenAlex.
- Regulation of water flow in the ocular lens: new roles for aquaporins.The Journal of physiology · 2024Review
- Design and Characterization of Model Systems that Promote and Disrupt Transparency of Vertebrate Crystallins In Vitro.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Replica exchange molecular dynamics simulations reveal self-association sites in M-crystallin caused by mutations provide insights of cataract.Scientific reports · 2021Article
- Improved SARS-CoV-2 PCR detection and genotyping with double-bubble primers.BioTechniques · 2021Article
- Application of 2D IR Bioimaging: Hyperspectral Images of Formalin-Fixed Pancreatic Tissues and Observation of Slow Protein Degradation.The journal of physical chemistry. B · 2021Article
- Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.Structure (London, England : 1993) · 2021Article
- The effects of cosolutes and crowding on the kinetics of protein condensate formation based on liquid-liquid phase separation: a pressure-jump relaxation study.Scientific reports · 2020Article
- MALDI imaging mass spectrometry of β- and γ-crystallins in the ocular lens.Journal of mass spectrometry : JMS · 2020Article
- Measuring Ultra-Weak Protein Self-Association by Non-ideal Sedimentation Velocity.Journal of the American Chemical Society · 2019Article
- Measuring macromolecular size distributions and interactions at high concentrations by sedimentation velocity.Nature communications · 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
- Amino acid composition in eyes from zebrafish (Danio rerio) and sardine (Sardina pilchardus) at the larval stage.SpringerPlus · 2016Article
- The Effect of Attractive Interactions and Macromolecular Crowding on Crystallins Association.PloS one · 2016Article
- 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
- Solution properties of γ-crystallins: hydration of fish and mammal γ-crystallins.Protein science : a publication of the Protein Society · 2014Article
- Structure and dynamics of the fish eye lens protein, γM7-crystallin.Biochemistry · 2013Article
- The molecular refractive function of lens γ-Crystallins.Journal of molecular biology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Crystallins are present in the lens at extremely high concentrations in order to provide transparency and generate a high refractive power of the lens. The crystallin families prevalent in the highest density lens tissues are γ-crystallins in vertebrates and S-crystallins in cephalopods. As shown elsewhere, in parallel evolution, both have evolved molecular refractive index increments 5-10% above those of most proteins. Although this is a small increase, it is statistically very significant and can be achieved only by very unusual amino acid compositions. In contrast, such a molecular adaptation to aid in the refractive function of the lens did not occur in crystallins that are preferentially located in lower density lens tissues, such as vertebrate α-crystallin and taxon-specific crystallins. In the current work, we apply a model of non-interacting hard spheres to examine the thermodynamic contributions of volume exclusion at lenticular protein concentrations. We show that the small concentration decrease afforded by the higher molecular refractive index increment of crystallins can amplify nonlinearly to produce order of magnitude differences in chemical activities, and lead to reduced osmotic pressure and the reduced propensity for protein aggregation. Quantitatively, this amplification sets in only at protein concentrations as high as those found in hard lenses or the nucleus of soft lenses, in good correspondence to the observed crystallin properties in different tissues and different species. This suggests that volume exclusion effects provide the evolutionary driving force for the unusual refractive properties and the unusual amino acid compositions of γ-crystallins and S-crystallins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.