Biology – Quantitative Biology – Biomolecules
Scientific paper
2008-11-27
Biosystems. 2008 Dec;94(3):248-52
Biology
Quantitative Biology
Biomolecules
Scientific paper
10.1016/j.biosystems.2008.06.016
We perform molecular dynamics simulations for a simple coarse-grained model of crambin placed inside of a softly repulsive sphere of radius R. The confinement makes folding at the optimal temperature slower and affects the folding scenarios, but both effects are not dramatic. The influence of crowding on folding are studied by placing several identical proteins within the sphere, denaturing them, and then by monitoring refolding. If the interactions between the proteins are dominated by the excluded volume effects, the net folding times are essentially like for a single protein. An introduction of inter-proteinic attractive contacts hinders folding when the strength of the attraction exceeds about a half of the value of the strength of the single protein contacts. The bigger the strength of the attraction, the more likely is the occurrence of aggregation and misfolding.
Cieplak Marek
Wojciechowski M.
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