Collapse transition of a hydrophobic self-avoiding random walk in a coarse-grained model solvent.
In order to study solvation effects on protein folding, we analyze the collapse transition of a self-avoiding random walk composed of hydrophobic segments that is embedded in a lattice model of a solvent. As expected, hydrophobic interactions lead to an attractive potential of mean force among chain segments. As a consequence, the random walk in solvent undergoes a collapse transition at a higher temperature than in its absence. Chain collapse is accompanied by the formation of a region depleted of solvent around the chain. In our simulation, the depleted region at collapse is as large as our computational domain.
Department of Physics, McGill University, Montreal, Quebec, Canada H3A 2T8.
Mathieu
M
Gaudreault
Jorge
J
Viñals
D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D012997:Solvents / Q000737:chemistry*
D012997:Solvents