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

doi 10.26434/chemrxiv.11336975.v1
Full Text
Abstract

Available in full text

Date
Authors
Publisher

American Chemical Society (ACS)

Related search

A Specific RNA Structural Motif Mediates High Affinity Binding by the HIV-1 Nucleocapsid Protein (NCp7)

Virology
Virology
1996English

Evaluating Parametrization Protocols for Hydration Free Energy Calculations With the AMOEBA Polarizable Force Field

Journal of Chemical Theory and Computation
Theoretical ChemistryComputer Science ApplicationsPhysical
2016English

Calculation of Protein-Ligand Binding Free Energy by Using a Polarizable Potential

Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
2008English

Identification of HIV-1 Inhibitors Targeting the Nucleocapsid Protein

Journal of Medicinal Chemistry
Drug DiscoveryMolecular Medicine
2012English

Improved Modeling of Halogenated Ligand-Protein Interactions Using the Drude Polarizable Force Field and Additive CHARMM36/CHARMM General Force Field (CGenFF)

Biophysical Journal
Biophysics
2019English

Polarizable Amoeba Force Field Metadynamics With Minimization Predicts Missing Protein Loops

Biophysical Journal
Biophysics
2017English

Examining the Stability of Β-Sheets Using the Charmm Drude Polarizable Force Field

Biophysical Journal
Biophysics
2017English

A Polarizable Reactive Force Field for Water to Enable Molecular Dynamics Simulations of Proton Transport

Journal of Chemical Physics
MedicineTheoretical ChemistryAstronomyPhysicsPhysical
2013English

A High Affinity Binding Site for the HIV-1 Nucleocapsid Protein

Nucleic Acids Research
Genetics
1997English

Amanote Research

Note-taking for researchers

Follow Amanote

© 2024 Amaplex Software S.P.R.L. All rights reserved.

Privacy PolicyRefund Policy