Molecular Dynamics Study on the Effect of Temperature on Deformation Mechanism of Magnesium Nanopillars with Square Cross-Sections

2016 ◽  
Vol 8 (7) ◽  
pp. 603-606 ◽  
Author(s):  
Shuang Xu ◽  
Ya-Fang Guo
Keyword(s):  
Molecular Dynamics ◽  
Cross Sections ◽  
Deformation Mechanism ◽  
Effect Of Temperature

Exploring secondary interactions and the role of temperature in moisture-contaminated polymer networks through molecular simulations

Soft Matter ◽  
2021 ◽  
Vol 17 (10) ◽  
pp. 2942-2956
Author(s):  
Rishabh D. Guha ◽  
Ogheneovo Idolor ◽  
Katherine Berkowitz ◽  
Melissa Pasquinelli ◽  
Landon R. Grace
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Temperature Variation ◽  
Polymer Networks ◽  
Molecular Simulations ◽  
Effect Of Temperature ◽  
Secondary Interactions ◽  
Dynamics Simulations ◽  
Secondary Bonding

We investigated the effect of temperature variation on the secondary bonding interactions between absorbed moisture and epoxies with different morphologies using molecular dynamics simulations.

Study on the effect of temperature and strain rate on Ni2FeCrCuAl high entropy alloy: a molecular dynamics study

2021 ◽  
Vol 3 (4) ◽  
pp. 045042
Author(s):  
S Gowthaman ◽  
T Jagadeesha
Keyword(s):  
Molecular Dynamics ◽  
Strain Rate ◽  
Point Defects ◽  
Tensile Deformation ◽  
Variable Temperature ◽  
Effect Of Temperature ◽  
High Entropy Alloy ◽  
High Entropy ◽  
Beneficial Impact ◽  
The Impact

Abstract High entropy alloy has offered significant attention in various material science applications, due to its excellent material features. In this investigation, the mechanical characteristics of Ni2FeCrCuAl High Entropy Alloy (HEA) have been examined under variable temperature and strain rates to analyze its influence over the material features of high entropy alloy through Molecular Dynamics (MD) simulation and it is stated that the formation of various point defects and dislocations are the major cause for the augmentation of tensile deformation which impacts the tensile behavior of high entropy alloy. Moreover, the Radial Distribution Function (RDF) has been examined throughout tensile deformation, to investigate the impact of applied stress over the de-bonding of various atoms and it is found that the strain rate has a greater beneficial impact over the material feature trailed by the temperature outcome, owed to its superior impact on the formation of point defects and shear strain during tensile characterization.

scholarly journals Molecular dynamics study of deformation mechanism of γ-TiAl intermetallics

2007 ◽  
Vol 56 (3) ◽  
pp. 1526
Author(s):  
Zhou Zong-Rong ◽  
Wang Yu ◽  
Xia Yuan-Ming
Keyword(s):  
Molecular Dynamics ◽  
Deformation Mechanism ◽  
Tial Intermetallics

scholarly journals Effects of the Temperature and the pH on the Main Protease of SARS-CoV-2: A Molecular Dynamics Simulation Study

2021 ◽  
Vol 12 (6) ◽  
pp. 7239-7248
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Root Mean Square ◽  
Dynamics Simulation ◽  
Effect Of Temperature ◽  
Water Molecules ◽  
Mean Square ◽  
Main Protease ◽  
Decreasing Ph ◽  
Increasing Temperature

The novel coronavirus, recognized as COVID-19, is the cause of an infection outbreak in December 2019. The effect of temperature and pH changes on the main protease of SARS-CoV-2 were investigated using all-atom molecular dynamics simulation. The obtained results from the root mean square deviation (RMSD) and root mean square fluctuations (RMSF) analyses showed that at a constant temperature of 25℃ and pH=5, the conformational change of the main protease is more significant than that of pH=6 and 7. Also, by increasing temperature from 25℃ to 55℃ at constant pH=7, a remarkable change in protein structure was observed. The radial probability of water molecules around the main protease was decreased by increasing temperature and decreasing pH. The weakening of the binding energy between the main protease and water molecules due to the increasing temperature and decreasing pH has reduced the number of hydrogen bonds between the main protease and water molecules. Finding conditions that alter the conformation of the main protease could be fundamental because this change could affect the virus’s functionality and its ability to impose illness.

scholarly journals How does temperature affect the dynamics of SARS-CoV-2 M proteins? Insights from Molecular Dynamics Simulations

2021 ◽  
Author(s):  
Soumya Lipsa Rath ◽  
Madhusmita Tripathy ◽  
Nabanita Mandal
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Membrane Lipids ◽  
Membrane System ◽  
Host Cells ◽  
Coarse Grained ◽  
M Protein ◽  
Effect Of Temperature ◽  
M Proteins ◽  
Dynamics Simulations

Enveloped viruses, in general, have several transmembrane proteins and glycoproteins, which assist the virus in entry and attachment onto the host cells. These proteins also play a significant role in determining the shape and size of the newly formed virus particles. The lipid membrane and the embedded proteins affect each other in non-trivial ways during the course of the viral life cycle. Unravelling the nature of the protein-protein and protein-lipid interactions, under various environmental and physiological conditions, could therefore prove to be crucial in development of therapeutics. Here, we study the M protein of SARS-CoV-2 to understand the effect of temperature on the properties of the protein-membrane system. The membrane embedded dimeric M proteins were studied using atomistic and coarse-grained molecular dynamics simulations at temperatures ranging between 10 and 50 ˚C. While temperature induced fluctuations should be monotonic, we observe a steady rise in the protein dynamics up to 40 ˚C, beyond which it surprisingly reverts back to the low temperature behaviour. Detailed investigation reveals disordering of the membrane lipids in the presence of the protein, which induces additional curvature around the transmembrane region. Coarse-grained simulations indicate temperature dependent aggregation of M protein dimers. Our study clearly indicates that the dynamics of membrane lipids and integral M protein of SARS-CoV-2 enables it to better associate and aggregate only at a certain temperature range (i.e., ~30 to 40 ˚C). This can have important implications in the protein aggregation and subsequent viral budding/fission processes.   

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