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

reportActive / Technical Report | Accession Number: AD1038265 | Open PDF

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.

Author(s):
Olson, Mark
Author Organization(s):
USAMRIID Ft Detrick United States
Descriptive Note:
Journal Article - Open Access
Supplementary Note:
ACS Journal of Chemical Information and Modeling , 01 Jan 0001, 01 Jan 0001,
Pagination:
0020

Security Markings

DOCUMENT & CONTEXTUAL SUMMARY

Distribution:
Approved For Public Release
Distribution Statement:
Approved For Public Release;

RECORD

Collection: TR
Identifying Numbers
Report Number(s):
DTRA/JSTO
 Subject Terms
Joint Capability Areas:
JCA_6_Net Centric; JCA_5.3_Planning; JCA_5_Command and Control; JCA_6.1.3_Switching and Routing; JCA_6.1_Information Transport; JCA_1.4_Force Support; JCA_1.4.1_Force Health Protection; JCA_3.2_Engagement; JCA_3_Force Application; JCA_3.2.2_Non-Kinetic Means; JCA_6.4_Information Assurance
Modernization Areas:
Quantum Science and Computing
Communities of Interest:
Energy and Power Technologies
Descriptor(s):
viruses, proteins, ebola virus, molecular dynamics simulations, biochemistry
Field(s)/Group(s):
Genetic Engineering and Molecular Biology
Report Date:
2017 Aug 10
Creation Date:
2017 Aug 10