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Crowding in the Eye Lens : Modeling the Multisubunit Protein β-Crystallin with a Colloidal Approach

Roosen-Runge, Felix LU ; Gulotta, Alessandro LU ; Bucciarelli, Saskia LU ; Casal-Dujat, Lucía LU ; Garting, Tommy LU ; Skar-Gislinge, Nicholas ; Obiols-Rabasa, Marc LU ; Farago, Bela ; Zaccarelli, Emanuela and Schurtenberger, Peter LU orcid , et al. (2020) In Biophysical Journal 119(12). p.2483-2496
Abstract

We present a multiscale characterization of aqueous solutions of the bovine eye lens protein βH crystallin from dilute conditions up to dynamical arrest, combining dynamic light scattering, small-angle x-ray scattering, tracer-based microrheology, and neutron spin echo spectroscopy. We obtain a comprehensive explanation of the observed experimental signatures from a model of polydisperse hard spheres with additional weak attraction. In particular, the model predictions quantitatively describe the multiscale dynamical results from microscopic nanometer cage diffusion over mesoscopic micrometer gradient diffusion up to macroscopic viscosity. Based on a comparative discussion with results from other crystallin proteins, we... (More)

We present a multiscale characterization of aqueous solutions of the bovine eye lens protein βH crystallin from dilute conditions up to dynamical arrest, combining dynamic light scattering, small-angle x-ray scattering, tracer-based microrheology, and neutron spin echo spectroscopy. We obtain a comprehensive explanation of the observed experimental signatures from a model of polydisperse hard spheres with additional weak attraction. In particular, the model predictions quantitatively describe the multiscale dynamical results from microscopic nanometer cage diffusion over mesoscopic micrometer gradient diffusion up to macroscopic viscosity. Based on a comparative discussion with results from other crystallin proteins, we suggest an interesting common pathway for dynamical arrest in all crystallin proteins, with potential implications for the understanding of crowding effects in the eye lens.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biophysical Journal
volume
119
issue
12
pages
14 pages
publisher
Cell Press
external identifiers
  • pmid:33189682
  • scopus:85096824707
ISSN
0006-3495
DOI
10.1016/j.bpj.2020.10.035
language
English
LU publication?
yes
id
85e0e242-f309-40f0-9798-f951fbe485c3
date added to LUP
2020-12-14 10:40:12
date last changed
2024-10-03 14:30:50
@article{85e0e242-f309-40f0-9798-f951fbe485c3,
  abstract     = {{<p>We present a multiscale characterization of aqueous solutions of the bovine eye lens protein β<sub>H</sub> crystallin from dilute conditions up to dynamical arrest, combining dynamic light scattering, small-angle x-ray scattering, tracer-based microrheology, and neutron spin echo spectroscopy. We obtain a comprehensive explanation of the observed experimental signatures from a model of polydisperse hard spheres with additional weak attraction. In particular, the model predictions quantitatively describe the multiscale dynamical results from microscopic nanometer cage diffusion over mesoscopic micrometer gradient diffusion up to macroscopic viscosity. Based on a comparative discussion with results from other crystallin proteins, we suggest an interesting common pathway for dynamical arrest in all crystallin proteins, with potential implications for the understanding of crowding effects in the eye lens.</p>}},
  author       = {{Roosen-Runge, Felix and Gulotta, Alessandro and Bucciarelli, Saskia and Casal-Dujat, Lucía and Garting, Tommy and Skar-Gislinge, Nicholas and Obiols-Rabasa, Marc and Farago, Bela and Zaccarelli, Emanuela and Schurtenberger, Peter and Stradner, Anna}},
  issn         = {{0006-3495}},
  language     = {{eng}},
  month        = {{12}},
  number       = {{12}},
  pages        = {{2483--2496}},
  publisher    = {{Cell Press}},
  series       = {{Biophysical Journal}},
  title        = {{Crowding in the Eye Lens : Modeling the Multisubunit Protein β-Crystallin with a Colloidal Approach}},
  url          = {{http://dx.doi.org/10.1016/j.bpj.2020.10.035}},
  doi          = {{10.1016/j.bpj.2020.10.035}},
  volume       = {{119}},
  year         = {{2020}},
}