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- W2891845306 abstract "Author(s): Prytkova, Vera Dmitrievna | Advisor(s): Tobias, Douglas J | Abstract: Realistic biological conditions are characterized by high concentrations of biomolecular solutes. Protein conformations and protein-protein interactions can be affected by crowding. The inclusion of a high number of proteins to model such environments necessitates the use of computationally inexpensive methods, such as rigid-body Brownian dynamics or Monte Carlo (MC) simulations. However, the rigid body representation of many protein systems gives rise to artifacts in protein-protein interactions. Presented here is the multi-conformational Monte Carlo (mcMC) method that avoids such artifacts by incorporating molecular flexibility at a low computational cost. We employ it to study the interaction of eye lens proteins, crystallins. In a healthy eye lens crystallins are the structure proteins. Their solubility at concentrations exceeding 400 mg/mL ensures lens transparency. The aggregation of crystallins leads to lens opacification, called cataract. We study how known point mutations associated with cataract formation lead to altered protein-protein interaction and creation of large aggregates." @default.
- W2891845306 created "2018-09-27" @default.
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- W2891845306 date "2018-01-01" @default.
- W2891845306 modified "2023-09-27" @default.
- W2891845306 title "Development of multiple conformation Monte Carlo method and its application to protein aggregation in cataract formation" @default.
- W2891845306 hasPublicationYear "2018" @default.
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