Molecular dynamics investigation of the size dependence of the heat of melting of metal nanoclusters

2014 ◽  
Vol 56 (12) ◽  
pp. 2369-2373 ◽  
Author(s):  
V. M. Samsonov ◽  
S. A. Vasilyev ◽  
A. G. Bembel ◽  
T. E. Samsonov ◽  
V. L. Skopich
Keyword(s):  
Molecular Dynamics ◽  
Size Dependence ◽  
Metal Nanoclusters

Size Dependence of the Melting Point of Silicon Nanoparticles: Molecular Dynamics and Thermodynamic Simulation

2019 ◽  
Vol 53 (7) ◽  
pp. 947-953 ◽  
Author(s):  
I. V. Talyzin ◽  
M. V. Samsonov ◽  
V. M. Samsonov ◽  
M. Yu. Pushkar ◽  
V. V. Dronnikov
Keyword(s):  
Molecular Dynamics ◽  
Melting Point ◽  
Silicon Nanoparticles ◽  
Size Dependence ◽  
Thermodynamic Simulation

Dielectric Relaxation in Small Confining Geometries

1994 ◽  
Vol 366 ◽  
Author(s):  
M. Arndt ◽  
F. Kremer
Keyword(s):  
Molecular Dynamics ◽  
Dielectric Loss ◽  
Dielectric Spectroscopy ◽  
Size Dependence ◽  
Dielectric Strength ◽  
Geometrical Constraint ◽  
Porous Glasses ◽  
Broadband Dielectric Spectroscopy ◽  
Inner Surface ◽  
Bulk Relaxation

ABSTRACTBroadband dielectric spectroscopy (10−2 Hz – 109 Hz) is employed to study the molecular dynamics of the glassforming liquid salol (phenyl salicylate) being contained in (dielectric inactive) porous glasses with pore sizes of about 2.5 nm, 5.0 nm and 7.5 nm. Besides the bulk relaxation (I) of salol, two further dielectric loss processes are observed due to the geometrical constraint of the inner surfaces of the pores: the “interfacial relaxation” (II) and a Maxwell-Wagner polarization (III). The “interfacial relaxation” is assigned to the restricted dynamics of the molecules close to the inner surface of the pores. It shows a strong pore-size dependence for pores < 5 nm both in relaxation rate and dielectric strength.

scholarly journals Comment on ‘Valid molecular dynamics simulations of human hemoglobin require a surprisingly large box size’

2019 ◽  
Author(s):  
Vytautas Gapsys ◽  
Bert L. de Groot
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Size Dependence ◽  
Conformational Transitions ◽  
Human Hemoglobin ◽  
Order Of Magnitude ◽  
The Stability ◽  
Dynamics Simulations ◽  
T State

AbstractA recent molecular dynamics investigation into the stability of hemoglobin concluded that the unliganded protein is only stable in the T state when a solvent box is used in the simulations that is ten times larger than what is usually employed. Here, we express three main concerns about that study. In addition, we show that with an order of magnitude more statistics, the reported box size dependence is not reproducible. Overall, no significant effects on the kinetics or thermodynamics of conformational transitions were observed.

scholarly journals Comment on 'Valid molecular dynamics simulations of human hemoglobin require a surprisingly large box size'

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Vytautas Gapsys ◽  
Bert L de Groot
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Size Dependence ◽  
Conformational Transitions ◽  
Human Hemoglobin ◽  
Order Of Magnitude ◽  
The Stability ◽  
Dynamics Simulations ◽  
T State

A recent molecular dynamics investigation into the stability of hemoglobin concluded that the unliganded protein is only stable in the T state when a solvent box is used in the simulations that is ten times larger than what is usually employed (El Hage et al., 2018). Here, we express three main concerns about that study. In addition, we find that with an order of magnitude more statistics, the reported box size dependence is not reproducible. Overall, no significant effects on the kinetics or thermodynamics of conformational transitions were observed.

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