Characterizing the Conformational Landscape of Flavivirus Fusion Peptides via Simulation and Experiment.

ABSTRACT: Conformational changes in the envelope proteins of flaviviruses help to expose the highly conserved fusion peptide (FP), a region which is critical to membrane fusion and host cell infection, and which represents a significant target for antiviral drugs and antibodies. In principle, extended timescale atomic-resolution simulations may be used to characterize the dynamics of such peptides. However, the resultant accuracy is critically dependent upon both the underlying force field and sufficient conformational sampling. In the present study, we report a comprehensive comparison of three simulation methods and four force fields comprising a total of more than 40 μs of sampling. Additionally, we describe the conformational landscape of the FP fold across all flavivirus family members. All inv

SUBMITTER: Marzinek JK 

PROVIDER: S-EPMC4726195 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature