期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 20, 期 28, 页码 19057-19070出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8cp03309a
关键词
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资金
- National Science Centre (NCN), Poland [2014/15/B/ST3/01905]
- EU Joint Programme in Neurodegenerative Diseases project through NCN [JPND CD FP-688-059, 2014/15/Z/NZ1/00037]
- NCN [2016/21/B/NZ1/00006]
- European Regional Development Fund under the Operational Programme Innovative Economy NanoFun [POIG.02.02.00-00-025/09]
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. In this model, inter-residue contacts form and disappear during the course of the time evolution. The contacts may arise between the sidechains, the backbones or the sidechains and backbones of the interacting residues. The model yields 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. In particular, the average radius of gyration scales with the sequence length in a residue-dependent manner.
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