Parallel Tempering of Dark Matter from the Ebola Virus Proteome: Comparison of CHARMM36m and CHARMM22 Force Fields with Implicit Solvent and Coarse-Grained Model
Abstract
Intrinsically disordered proteins are characterized by their large manifold of thermally accessible conformations and their related statistical weights making them an interesting target of simulation studies. To assess the development of a computational framework for modeling this class of proteins, this work examines temperature-based replica exchange simulations to generate a conformational ensemble of a disordered 28-residue peptide from the Ebola virus protein VP35 starting from a prefolded helix beta-turn-helix topology observed in a viral assembly.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 10, 2017
- Accession Number
- AD1038265
Entities
People
- Mark A Olson
Organizations
- United States Army Medical Research Institute of Infectious Diseases