Elucidating thermal behavior, native contacts, and folding funnels of simple lattice proteins using replica exchange Wang-Landau sampling

2018 ◽  
Vol 149 (16) ◽  
pp. 164913
Author(s):  
Guangjie Shi ◽  
Thomas Wüst ◽  
David P. Landau
Keyword(s):  
Thermal Behavior ◽  
Replica Exchange ◽  
Simple Lattice ◽  
Lattice Proteins

scholarly journals Free energy approximations in simple lattice proteins

2001 ◽  
Vol 114 (11) ◽  
pp. 4998-5005
Author(s):  
Dirk Reith ◽  
Thomas Huber ◽  
Florian Müller-Plathe ◽  
Andrew E. Torda
Keyword(s):  
Free Energy ◽  
Simple Lattice ◽  
Lattice Proteins

Computational Investigations of the Transmembrane Italian-Mutant (E22K) 3A\(\beta_{11 - 40}\) in Aqueous Solution

2018 ◽  
Vol 28 (3) ◽  
pp. 265 ◽  
Author(s):  
Son Tung Ngo
Keyword(s):  
Structural Changes ◽  
Replica Exchange ◽  
Aβ Oligomers ◽  
Replica Exchange Molecular Dynamics ◽  
Charged Residue ◽  
Intermolecular Contacts ◽  
Structural Details ◽  
Positively Charged ◽  
Dynamic Fluctuation ◽  
Good Agreement

The Amyloid beta (Aβ) oligomers are characterized as critical cytotoxic materials in Alzheimer’s disease (AD) pathogenesis. Structural details of transmembrane oligomers are inevitably necessary to design/search potential inhibitor due to treat AD. However, the experimental detections for structural modify of low-order Aβ oligomers are precluded due to the extremely dynamic fluctuation of the oligomers. In this project, the transmembrane Italian-mutant (E22K) 3Aβ11-40 (tmE22K 3Aβ11-40) was extensively investigated upon the temperature replica exchange molecular dynamics (REMD) simulations. The structural changes of the trimer when replacing the negative charged residue E22 by a positively charged residue K were monitored over simulation intervals. The oligomer size was turned to be larger and the increase of β-content was recorded. The momentous gain of intermolecular contacts with DPPC molecules implies that tmE22K 3Aβ11-40 easier self-inserts into the membrane than the WT one. Furthermore, the tighter interaction between constituting monomers was indicated implying that the E22K mutation probably enhances the Aβ fibril formation. The results are in good agreement with experiments that E22K amyloid is self-aggregate faster than the WT form. Details information of tmE22K trimer structure and kinetics probably yield the understanding of AD mechanism.

Comparative analysis of butter thermal behavior in combination with bovine tallow

2020 ◽  
Vol 40 (suppl 2) ◽  
pp. 597-604
Author(s):  
Zahra NILCHIAN ◽  
Mohamad Reza EHSANI ◽  
Zahra PIRAVI-VANAK ◽  
Hossein BAKHODA
Keyword(s):  
Comparative Analysis ◽  
Thermal Behavior

NUMERICAL AND EXPERIMENTAL STUDY OF TRANSIENT THERMAL BEHAVIOR OF ELECTRONIC INFRARED RADIATION CONTROL MODULE

2019 ◽  
Vol 50 (17) ◽  
pp. 1721-1736
Author(s):  
Kaiqiang Hou ◽  
Xiaolong Weng ◽  
Wei Luo ◽  
Le Yuan ◽  
Wei Duan ◽  
...  
Keyword(s):  
Experimental Study ◽  
Thermal Behavior ◽  
Infrared Radiation ◽  
Control Module ◽  
Radiation Control ◽  
Transient Thermal
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