Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2020 Nov 27:1–12. doi: 10.1080/07391102.2020.1846626

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2020 Informa UK Limited, trading as Taylor & Francis Group

This article is made available via the PMC Open Access Subset for unrestricted re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the COVID-19 pandemic or until permissions are revoked in writing. Upon expiration of these permissions, PMC is granted a perpetual license to make this article available via PMC and Europe PMC, consistent with existing copyright protections.

PMC Copyright notice

Figure 5. — Molecular docking and molecular dynamics simulations studies. (A and B) The molecular interaction studies of vaccine candidate with immune receptor TLR3 using HDOCK server was performed and different representation of the vaccine (orange) and TLR3 receptor (orange) are shown here. Molecular dynamics simulation of vaccine and immune receptor TLR3 complex was done for 100 ns using GROMACS. (A) RMSD (root mean square deviation) plots reflect the stability between the vaccine candidate and TLR-3 receptor whereas (B) RMSF (root mean square fluctuation) reflecting the flexibility and fluctuation of the residual atoms in the side chain of docked complex. (C) Radius of gyration is plotted as a function of time to know the structural compactness. (D) Hydrogen bonds of the complex are graphically represented to study the changes in stability of vaccine-receptor complex.