December 2002
Volume 43, Issue 13
Free
ARVO Annual Meeting Abstract  |   December 2002
Comparison of Monte Carlo Simulations with X-ray Scattering from High Concentration Mixtures of Alpha and Gamma-B Crystallins
Author Affiliations & Notes
  • GM Thurston
    Center for Ophthalmic Research Brigham and Womens Hospital Boston MA
  • V Lobaskin
    Physics U Fribourg Fribourg Switzerland
  • L Lurio
    Physics U Northern Illinois DeKalb IL
  • P Schurtenberger
    Physics U Fribourg Fribourg Switzerland
  • S Mochrie
    Physics Yale University New Haven CT
  • Footnotes
    Commercial Relationships   G.M. Thurston, None; V. Lobaskin, None; L. Lurio, None; P. Schurtenberger, None; S. Mochrie, None. Grant Identification: Support: NIH Grant EY11840. 8-ID is supported by DOE (DE-FG02-96ER45593) and NSF (DMR 9312543).
Investigative Ophthalmology & Visual Science December 2002, Vol.43, 4655. doi:
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    • Get Citation

      GM Thurston, V Lobaskin, L Lurio, P Schurtenberger, S Mochrie; Comparison of Monte Carlo Simulations with X-ray Scattering from High Concentration Mixtures of Alpha and Gamma-B Crystallins . Invest. Ophthalmol. Vis. Sci. 2002;43(13):4655.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Abstract: : Purpose:To study whether X-ray scattering data, reflecting the liquid structure of high concentration α and γ B crystallin mixtures, can be reproduced by Monte Carlo simulation of particles interacting via simple, appropriate model potentials. Methods:Model γ B-γ B interactions combined hard-core repulsion of effective spheres with an attractive Yukawa potential . α-α and α-γ B interactions were represented by hard-core repulsion alone. The Yukawa range and depth were chosen using the known critical volume fraction and critical temperature for γ B-crystallin. Effective sphere sizes were chosen using the known molecular volume of γ B, and the radius of gyration observed by X-ray scattering for α. For X-ray scattering, calf lens proteins were isolated using size-exclusion and ion-exchange chromatography, concentrated by ultrafiltration, and analyzed in solutions containing 0.1 M sodium phosphate buffer, pH 7.1, with 20mM dithiothreitol. The X-ray scattering intensity, I(q), as a function of wavevector, q, was measured in the range 0.04 < q < 6 nm-1, using Beamline 8-ID at the Advanced Photon Source. Results:We find nearly quantitative agreement between the simulated I(q) and the measured I(q), at a total protein concentration of 260 mg/ml, for α-crystallin relative proportions ranging from 0 to 1. Refinements to incorporate more realistic γ B-crystallin shape may be needed. Conclusion:Simple model potentials such as these can provide useful starting points for understanding the liquid structure of lens crystallin mixtures, at concentrations comparable to those in the eye lens.

Keywords: 378 crystallins 
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