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Hydropathic wave ordering of alpha crystallin—Membrane interactions enhances human lens transparency and resists cataracts

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  • Moret, M.A.
  • Zebende, G.F.
  • Phillips, J.C.

Abstract

Granted that neural networks are nature’s most amazing invention, what is in second place? One candidate is the human eye, and specifically its transparent lens. Here we use the evolution of the lens’ dominant proteins to quantify subtle improvements in alpha crystallins between chickens and humans. These improvements are different in αA and αB crystallins, and suggest that their functions are complementary. We relate crystallin evolution to the fiber cell structure of the eye, and its enhanced resistance to cataracts in humans, with weakened resistance in rats, which improves to elephants and finally humans. Our results show that the 2007 Brazilian hydropathicity scale based on self-organized criticality is qualitatively superior to the >100 classical scales based on protein unfolding.

Suggested Citation

  • Moret, M.A. & Zebende, G.F. & Phillips, J.C., 2019. "Hydropathic wave ordering of alpha crystallin—Membrane interactions enhances human lens transparency and resists cataracts," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 514(C), pages 573-579.
    • Handle: RePEc:eee:phsmap:v:514:y:2019:i:c:p:573-579
    DOI: 10.1016/j.physa.2018.09.128
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    References listed on IDEAS

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    1. Phillips, J.C., 2017. "Hidden thermodynamic information in protein amino acid mutation tables," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 469(C), pages 676-680.
    2. Allan, Douglas C. & Phillips, J.C., 2017. "Evolution of the ubiquitin-activating enzyme Uba1 (E1)," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 483(C), pages 456-461.
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