Accession Number:

AD1038265

Title:

Parallel Tempering of Dark Matter from the Ebola Virus Proteome: Comparison of CHARMM36m and CHARMM22 Force Fields with Implicit Solvent and Coarse-Grained Model

Descriptive Note:

Journal Article - Open Access

Corporate Author:

USAMRIID Ft Detrick United States

Personal Author(s):

• Olson,Mark

Report Date:

2017-08-10

Pagination or Media Count:

20.0

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.

Descriptors:

• viruses
• proteins
• ebola virus
• molecular dynamics simulations
• biochemistry

Subject Categories:

• Genetic Engineering and Molecular Biology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE