Skip to Main content Skip to Navigation
Journal articles

Reconciling NMR Structures of the HIV-1 Nucleocapsid Protein (NCp7) using Extensive Polarizable Force Field Free-Energy Simulations

Abstract : Using polarizable (AMOEBA) and non-polarizable (CHARMM) force fields, we compare the relative free energy stability of two extreme conformations of the HIV-1 NCp7 nucleocapsid that had been previously experimentally advocated to prevail in solution. Using accelerated sampling techniques, we show that they differ in stability by no more than 0.75-1.9 kcal/mol depending on the reference protein sequence. While the extended form appears to be the most probable structure, both forms should thus coexist in water explaining the differing NMR findings.
Document type :
Journal articles
Complete list of metadatas

https://hal.archives-ouvertes.fr/hal-02377723
Contributor : Jean-Philip Piquemal <>
Submitted on : Sunday, November 24, 2019 - 11:28:25 AM
Last modification on : Friday, October 23, 2020 - 3:24:47 AM

Identifiers

Citation

L. El Khoury, F. Célerse, Louis Lagardère, L.-.H Jolly, E. Derat, et al.. Reconciling NMR Structures of the HIV-1 Nucleocapsid Protein (NCp7) using Extensive Polarizable Force Field Free-Energy Simulations. Journal of Chemical Theory and Computation, American Chemical Society, 2020, 16 (4), pp.2013-2020. ⟨10.1021/acs.jctc.9b01204⟩. ⟨hal-02377723⟩

Share

Metrics

Record views

403