ReaxFF molecular dynamics simulation of thermal stability of a Cu3(BTC)2 metal–organic framework

2012 ◽  
Vol 14 (32) ◽  
pp. 11327 ◽  
Author(s):  
Liangliang Huang ◽  
Kaushik L. Joshi ◽  
Adri C. T. van Duin ◽  
Teresa J. Bandosz ◽  
Keith E. Gubbins
Keyword(s):  
Molecular Dynamics ◽  
Thermal Stability ◽  
Molecular Dynamics Simulation ◽  
Metal Organic Framework ◽  
Dynamics Simulation ◽  
Metal Organic ◽  
Thermal Stability Of ◽  
Organic Framework

Reactive adsorption of ammonia and ammonia/water on CuBTC metal-organic framework: A ReaxFF molecular dynamics simulation

2013 ◽  
Vol 138 (3) ◽  
pp. 034102 ◽  
Author(s):  
Liangliang Huang ◽  
Teresa Bandosz ◽  
Kaushik L. Joshi ◽  
Adri C. T. van Duin ◽  
Keith E. Gubbins
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Metal Organic Framework ◽  
Dynamics Simulation ◽  
Ammonia Water ◽  
Reactive Adsorption ◽  
Metal Organic ◽  
Organic Framework

Porous homo- and heterochiral cobalt(II) aspartates with high thermal stability of the metal-organic framework

2010 ◽  
Vol 59 (4) ◽  
pp. 733-740 ◽  
Author(s):  
M. P. Yutkin ◽  
M. S. Zavakhina ◽  
D. G. Samsonenko ◽  
D. N. Dybtsev ◽  
V. P. Fedin
Keyword(s):  
Thermal Stability ◽  
Metal Organic Framework ◽  
High Thermal Stability ◽  
Metal Organic ◽  
Thermal Stability Of ◽  
Organic Framework

scholarly journals Molecular Dynamics Simulation of Barnase: Contribution of Noncovalent Intramolecular Interaction to Thermostability

2013 ◽  
Vol 2013 ◽  
pp. 1-12 ◽  
Author(s):  
Zhiguo Chen ◽  
Yi Fu ◽  
Wenbo Xu ◽  
Ming Li
Keyword(s):  
Molecular Dynamics ◽  
Thermal Stability ◽  
Molecular Dynamics Simulation ◽  
Root Mean Square ◽  
Clinical Medicine ◽  
Intramolecular Interaction ◽  
Salt Bridge ◽  
Dynamics Simulation ◽  
Mean Square ◽  
Thermal Stability Of

Bacillus amyloliquefaciensribonuclease Barnase (RNase Ba) is a 12 kD (kilodalton) small extracellular ribonuclease. It has broad application prospects in agriculture, clinical medicine, pharmaceutical, and so forth. In this work, the thermal stability of Barnase has been studied using molecular dynamics simulation at different temperatures. The present study focuses on the contribution of noncovalent intramolecular interaction to protein stability and how they affect the thermal stability of the enzyme. Profiles of root mean square deviation and root mean square fluctuation identify thermostable and thermosensitive regions of Barnase. Analyses of trajectories in terms of secondary structure content, intramolecular hydrogen bonds and salt bridge interactions indicate distinct differences in different temperature simulations. In the simulations, Four three-member salt bridge networks (Asp8-Arg110-Asp12, Arg83-Asp75-Arg87, Lys66-Asp93-Arg69, and Asp54-Lys27-Glu73) have been identified as critical salt bridges for thermostability which are maintained stably at higher temperature enhancing stability of three hydrophobic cores. The study may help enlighten our knowledge of protein structural properties, noncovalent interactions which can stabilize secondary peptide structures or promote folding, and also help understand their actions better. Such an understanding is required for designing efficient enzymes with characteristics for particular applications at desired working temperatures.

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