scholarly journals Key residues in TLR4-MD2 tetramer formation identified by free energy simulations

2019 ◽  
Vol 15 (10) ◽  
pp. e1007228 ◽  
Author(s):  
Alireza Tafazzol ◽  
Yong Duan
Keyword(s):  
Free Energy ◽  
Tetramer Formation ◽  
Energy Simulations ◽  
Key Residues

Prediction of Alkanolamine pKa Values by Combined Molecular Dynamics Free Energy Simulations and ab initio Calculations

2019 ◽  
Author(s):  
Javad Noroozi ◽  
William Smith
Keyword(s):  
Molecular Dynamics ◽  
Free Energy ◽  
Ab Initio Calculations ◽  
Gas Phase ◽  
Quantum Chemical ◽  
Phase Reaction ◽  
Pka Values ◽  
Gas Phase Reaction ◽  
Reaction Free Energy ◽  
Energy Simulations

We use molecular dynamics free energy simulations in conjunction with quantum chemical calculations of gas phase reaction free energy to predict alkanolamines pka values. <br>

scholarly journals Analysis of Phosphoryl-Transfer Enzymes with QM/MM Free Energy Simulations

2018 ◽  
pp. 53-90 ◽  
Author(s):  
Daniel Roston ◽  
Xiya Lu ◽  
Dong Fang ◽  
Darren Demapan ◽  
Qiang Cui
Keyword(s):  
Free Energy ◽  
Phosphoryl Transfer ◽  
Energy Simulations

Specific amino acid recognition by aspartyl-tRNA synthetase studied by free energy simulations 1 1A. R. Fersht

1998 ◽  
Vol 275 (5) ◽  
pp. 823-846 ◽  
Author(s):  
Georgios Archontis ◽  
Thomas Simonson ◽  
Dino Moras ◽  
Martin Karplus
Keyword(s):  
Free Energy ◽  
Amino Acid ◽  
Trna Synthetase ◽  
Specific Amino Acid ◽  
Energy Simulations ◽  
Amino Acid Recognition

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

2020 ◽  
Author(s):  
Léa El Khoury ◽  
Frédéric Célerse ◽  
Louis Lagardere ◽  
Luc-Henri Jolly ◽  
Étienne Derat ◽  
...  
Keyword(s):  
Free Energy ◽  
Nucleocapsid Protein ◽  
Extended Form ◽  
Polarizable Force Field ◽  
Relative Free Energy ◽  
Nmr Structures ◽  
Reference Protein ◽  
Energy Simulations ◽  
Hiv 1 ◽  
Most Probable Structure

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.<br>

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