Disordered peptide chains in a coarse-grained model

We construct a one-bead-per-residue coarse-grained dynamical model
to describe intrinsically disordered proteins at significantly longer
timescales than in the all-atom models. It yields structural
results that are consistent with many all-atom and experimental
data on these systems. We demonstrate that the geometrical properties
of various homopeptides differ substantially in this model.
The (breakable) contacts between the beads are determined during
the course of the time evolution.\\


[1] L. Mioduszewski and M. Cieplak, PCCP 20, 19057 (2018)