Formation and Evolution of Icosahedron during Relaxation of Amorphous Ca7Mg3 Alloy

2014 ◽  
Vol 651-653 ◽  
pp. 241-244
Author(s):  
Li Li Zhou ◽  
Chong Xing ◽  
You Lin Peng
Keyword(s):  
Experimental Data ◽  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Microstructure Evolution ◽  
Structure Factor ◽  
Isothermal Annealing ◽  
Dynamics Simulation ◽  
Simulation Studies ◽  
Structure Transformation ◽  
Formation And Evolution

The molecular dynamics simulation studies on the microstructure evolution properties of amorphous Ca7Mg3 alloy during the isothermal annealing have been performed. The simulated structure factor S(q) of Ca7Mg3 is well agreed with the experimental data. Results indicate that the icosahedron structure plays dominate role in the structure transformation, and the smaller Mg atoms are much more probable to be the central atoms of the basic clusters of icosahedron.

Structure Relaxations during the Isothermal Annealing of Amorphous Ca7Mg3 Alloy

2013 ◽  
Vol 813 ◽  
pp. 51-54
Author(s):  
Li Li Zhou ◽  
You Lin Peng ◽  
Hui Luo ◽  
Rang Su Liu
Keyword(s):  
Experimental Data ◽  
Molecular Dynamics ◽  
Short Range ◽  
Short Range Order ◽  
Isothermal Annealing ◽  
Amorphous Structure ◽  
Annealing Process ◽  
Range Order ◽  
Dynamics Simulation ◽  
Simulation Studies

The molecular dynamics simulation studies on the microstructure evolution properties of amorphous Ca7Mg3 alloy during the isothermal annealing have been performed. The simulated structure factor S(q) of Ca7Mg3 is well agreed with the experimental data. Results indicate that the metallic glass of Ca7Mg3 alloy is relaxed into amorphous structure of greater stability in which much more icosahedron structures is formed; interestingly, it is also found that the short short-range order has no change, while the short-range order of the system increases during the isothermal annealing process.

scholarly journals Computational Investigations on the Binding Mode of Ligands for the Cannabinoid-Activated G Protein-Coupled Receptor GPR18

Biomolecules ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 686 ◽  
Author(s):  
Alexander Neumann ◽  
Viktor Engel ◽  
Andhika B. Mahardhika ◽  
Clara T. Schoeder ◽  
Vigneshwaran Namasivayam ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
G Protein ◽  
Phenyl Ring ◽  
Binding Mode ◽  
Dynamics Simulation ◽  
Simulation Studies ◽  
Binding Modes ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

GPR18 is an orphan G protein-coupled receptor (GPCR) expressed in cells of the immune system. It is activated by the cannabinoid receptor (CB) agonist ∆9-tetrahydrocannabinol (THC). Several further lipids have been proposed to act as GPR18 agonists, but these results still require unambiguous confirmation. In the present study, we constructed a homology model of the human GPR18 based on an ensemble of three GPCR crystal structures to investigate the binding modes of the agonist THC and the recently reported antagonists which feature an imidazothiazinone core to which a (substituted) phenyl ring is connected via a lipophilic linker. Docking and molecular dynamics simulation studies were performed. As a result, a hydrophobic binding pocket is predicted to accommodate the imidazothiazinone core, while the terminal phenyl ring projects towards an aromatic pocket. Hydrophobic interaction of Cys251 with substituents on the phenyl ring could explain the high potency of the most potent derivatives. Molecular dynamics simulation studies suggest that the binding of imidazothiazinone antagonists stabilizes transmembrane regions TM1, TM6 and TM7 of the receptor through a salt bridge between Asp118 and Lys133. The agonist THC is presumed to bind differently to GPR18 than to the distantly related CB receptors. This study provides insights into the binding mode of GPR18 agonists and antagonists which will facilitate future drug design for this promising potential drug target.

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