Self-organizing domains in conformations of Ebola virus protein VP40

Conformational variations of an ebola virus protein (VP40) as a function of temperature (T) are studied by coarse-grained Monte Carlo (MC) and Molecular Dynamics simulations. A number of local and global physical quatities are examined including contact map, radius of gyration, structure factor etc. We find that the self-organizing residues leads to onset of domains with globular conformations at low temperatures. Domains are localized around N-tail, intermediate region, and C-terminal at low temperature but disappear at high temperature where the protein is denatured into a random coil conformation. Response of the domain dynamics as a function of temperature shows that the N-terminal domain is most stable and perhaps critical in latching mechanism of the ebola virus.