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- W2903185701 abstract "Steric interactions with surrounding macromolecules tend to favor the compact native state of a globular protein over its unfolded state. However, in experiments conducted in cells and concentrated protein solutions, both stabilization and destabilization of proteins have been observed, compared to dilute-solution conditions. Therefore, in order to understand the effects of surrounding macromolecules on protein properties such as stability, there is a need for computational modeling beyond the level of hard-sphere crowders. Here, we discuss some recent exploratory studies of peptide folding in the presence of explicit protein crowders, carried out by us using an all-atom Monte Carlo-based approach along with an implicit solvent force field. For interpreting the simulation data, time-lagged independent component analysis and Markov state modeling are used." @default.
- W2903185701 created "2018-12-11" @default.
- W2903185701 creator A5050478272 @default.
- W2903185701 creator A5060442147 @default.
- W2903185701 creator A5089826765 @default.
- W2903185701 date "2018-11-29" @default.
- W2903185701 modified "2023-09-27" @default.
- W2903185701 title "Peptide Folding in Cellular Environments: A Monte Carlo and Markov Modeling Approach" @default.
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- W2903185701 doi "https://doi.org/10.1007/978-3-319-95843-9_13" @default.
- W2903185701 hasPublicationYear "2018" @default.
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