Journal
JOURNAL OF COMPUTATIONAL CHEMISTRY
Volume 44, Issue 19, Pages 1658-1666Publisher
WILEY
DOI: 10.1002/jcc.27116
Keywords
cataract; crystallins; molecular dynamics simulations; Monte Carlo simulations; protein solubility
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Using atomistic multiscale molecular simulations, we investigated the solution-state conformational dynamics and interprotein interactions of ?D-crystallin and its P23T-R36S mutant. We found that the mutant retains the protein fold but exhibits changes in surface exposure of residues, leading to enhanced protein-protein interactions and specific contacts observed in the protein crystal lattice.
The molecular basis underlying the rich phase behavior of globular proteins remains poorly understood. We use atomistic multiscale molecular simulations to model the solution-state conformational dynamics and interprotein interactions of ?D-crystallin and its P23T-R36S mutant, which drastically limits the protein solubility, at both infinite dilution and at a concentration where the mutant fluid phase and crystalline phase coexist. We find that while the mutant conserves the protein fold, changes to the surface exposure of residues in the neighborhood of residue-36 enhance protein-protein interactions and develop specific protein-protein contacts found in the protein crystal lattice.
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