Evidence map›Paper›PMID 28178791›Full record

ArticleThe Journal of chemical physics2017

Statistical-thermodynamic model for light scattering from eye lens protein mixtures.

Michael M Bell, David S Ross, Maurino P Bautista, Hossein Shahmohamad, Andreas Langner, John F Hamilton, Carrie N Lahnovych, George M Thurston

Abstract read
In one paragraph

Article in The Journal of chemical physics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Michael M BellSchool of Mathematical Sciences, Rochester Institute of Technology, Rochester, New York 14623, USA.
David S RossSchool of Mathematical Sciences, Rochester Institute of Technology, Rochester, New York 14623, USA.
Maurino P BautistaSchool of Mathematical Sciences, Rochester Institute of Technology, Rochester, New York 14623, USA.
Hossein ShahmohamadSchool of Mathematical Sciences, Rochester Institute of Technology, Rochester, New York 14623, USA.
Andreas LangnerSchool of Chemistry and Materials Science, Rochester Institute of Technology, Rochester, New York 14623, USA.
John F HamiltonSchool of Mathematical Sciences, Rochester Institute of Technology, Rochester, New York 14623, USA.
Carrie N LahnovychSchool of Mathematical Sciences, Rochester Institute of Technology, Rochester, New York 14623, USA.
George M ThurstonSchool of Physics and Astronomy, Rochester Institute of Technology, Rochester, New York 14623, USA.

Funding

Phase boundaries and liquid structure of concentrated eye lens protein mixturesR15EY018249 · NEI · ROCHESTER INSTITUTE OF TECHNOLOGY · PI THURSTON, GEORGE · 2008 to 2013
$572k
NEI NIH HHS R15 EY018249
6 · The paper itself

Abstract

We model light-scattering cross sections of concentrated aqueous mixtures of the bovine eye lens proteins γB- and α-crystallin by adapting a statistical-thermodynamic model of mixtures of spheres with short-range attractions. The model reproduces measured static light scattering cross sections, or Rayleigh ratios, of γB-α mixtures from dilute concentrations where light scattering intensity depends on molecular weights and virial coefficients, to realistically high concentration protein mixtures like those of the lens. The model relates γB-γB and γB-α attraction strengths and the γB-α size ratio to the free energy curvatures that set light scattering efficiency in tandem with protein refractive index increments. The model includes (i) hard-sphere α-α interactions, which create short-range order and transparency at high protein concentrations, (ii) short-range attractive plus hard-core γ-γ interactions, which produce intense light scattering and liquid-liquid phase separation in aqueous γ-crystallin solutions, and (iii) short-range attractive plus hard-core γ-α interactions, which strongly influence highly non-additive light scattering and phase separation in concentrated γ-α mixtures. The model reveals a new lens transparency mechanism, that prominent equilibrium composition fluctuations can be perpendicular to the refractive index gradient. The model reproduces the concave-up dependence of the Rayleigh ratio on α/γ composition at high concentrations, its concave-down nature at intermediate concentrations, non-monotonic dependence of light scattering on γ-α attraction strength, and more intricate, temperature-dependent features. We analytically compute the mixed virial series for light scattering efficiency through third order for the sticky-sphere mixture, and find that the full model represents the available light scattering data at concentrations several times those where the second and third mixed virial contributions fail. The model indicates that increased γ-γ attraction can raise γ-α mixture light scattering far more than it does for solutions of γ-crystallin alone, and can produce marked turbidity tens of degrees celsius above liquid-liquid separation.

Indexed as

Thermodynamicsalpha-CrystallinsAnimalsCattlegamma-CrystallinsLens, CrystallineModels, BiologicalModels, StatisticalScattering, Radiationalpha-Crystallinsgamma-Crystallins

Identifiers

PMID28178791
PMCPMC5291805

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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.