June 2013
Volume 54, Issue 15
Free
ARVO Annual Meeting Abstract  |   June 2013
Statistical-thermodynamic model for charge-regulation properties of bovine γB-crystallin
Author Affiliations & Notes
  • George Thurston
    Physics, Rochester Institute of Technology, Rochester, NY
  • Michael Martini
    Physics, Rochester Institute of Technology, Rochester, NY
    Physics, University of Illinois at Urbana-Champaign, Urbana-Champaign, IL
  • Chris Wahle
    Mathematics, Rochester Institute of Technology, Rochester, NY
  • Dawn Hollenbeck
    Physics, Rochester Institute of Technology, Rochester, NY
  • David Ross
    Mathematics, Rochester Institute of Technology, Rochester, NY
  • John Hamilton
    Mathematics, Rochester Institute of Technology, Rochester, NY
  • Footnotes
    Commercial Relationships George Thurston, None; Michael Martini, None; Chris Wahle, None; Dawn Hollenbeck, None; David Ross, None; John Hamilton, None
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science June 2013, Vol.54, 4965. doi:
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    • Get Citation

      George Thurston, Michael Martini, Chris Wahle, Dawn Hollenbeck, David Ross, John Hamilton; Statistical-thermodynamic model for charge-regulation properties of bovine γB-crystallin. Invest. Ophthalmol. Vis. Sci. 2013;54(15):4965.

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

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Abstract
 
Purpose
 

To model interacting-site protonation equilibria of γB-crystallin to aid in quantifying screened, charge-regulated electrostatic γB-γB interactions.

 
Methods
 

We model screened, site-specific charge regulation in γB-crystallin and neighboring pairs of γB-crystallin molecules, adapting our recent formulation (Hollenbeck et al, Phys. Rev. E 2010) to use γB-crystallin crystallographic coordinates. Using a simplified dielectric model, we solve a screened electrostatic partial differential equation model to calculate a 51 x 51 work-of-charging matrix, and use relevant data to model site-specific proton affinities. We use Monte Carlo simulations to calculate the grand canonical partition function and the probabilities of leading proton occupancy configurations, for 4 < pH < 8 and Debye screening length values from 6 to 30 Angstroms.

 
Results
 

The work of charging matrix can be put into an approximate block-diagonal form in which blocks correspond to interacting patches of titratable sites that include long-recognized charge pairing in γB-crystallin. The predicted average net protein charge fits available near-neutral pH potentiometric titration data on γB-crystallin reasonably well, but deviates at low and high pH. For neighboring γB molecule pairs, the relevant 102x102 enlarged work-of-charging matrix depends on relative intermolecular proximity and orientation, making protonation configurations interdependent for near neighbors. At pH 7.0 and Debye length 6 Angstroms, the most prominent γB-crystallin proton occupancy configuration is only predicted to occur less than a tenth of the time, the first hundred configurations account for only 75% of the total, and nearly a thousand are needed to account for 95%. Proton occupancy probability distributions broaden remarkably as pH is lowered to close to 4.5, then sharpen again; over a thousand configurations account for only 30% of the total at pH 4.5. Raising the Debye screening length considerably sharpens the proton configuration probability distributions, due to strengthened site-site interactions.

 
Conclusions
 

The broad width of γB-crystallin proton occupancy probability distributions, and their interdependence in neighboring γB molecules, suggest that charge regulation is one important aspect of screened electrostatic contributions to orientation-dependent γB-γB interactions.

 
 
Modeled γB-crystallin proton occupancy statistics for Debye length 6Å
 
Modeled γB-crystallin proton occupancy statistics for Debye length 6Å
 
Keywords: 488 crystallins • 659 protein structure/function  
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