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10.1063/5.0055331 http://scihub22266oqcxt.onion/10.1063/5.0055331 34241335!ä!34241335 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Chem+Phys 2021 ; 154 (24): 245101 Nephropedia Template TP {{tp|p=34241335|t=2021. The role of the envelope protein in the stability of a coronavirus model membrane against an ethanolic disinfectant |pdf=|usr=}}{{34241335}} gab.com Text The role of the envelope protein in the stability of a coronavirus model membrane against an ethanolic disinfectant JO: J Chem Phys http://www.kidney.de/pget.php?&tw=1&pmid=34241335 #FOAvip Ethanol is highly effective against various enveloped viruses and can disable the virus by disintegrating the protective envelope surrounding it. The interactions between the coronavirus envelope (E) protein and its membrane environment play key roles in the stability and function of the viral envelope. By using molecular dynamics simulation, we explore the underlying mechanism of ethanol-induced disruption of a model coronavirus membrane and, in detail, interactions of the E-protein and lipids. We model the membrane bilayer as N-palmitoyl-sphingomyelin and 1-palmitoyl-2-oleoylphosphatidylcholine lipids and the coronavirus E-protein. The study reveals that ethanol causes an increase in the lateral area of the bilayer along with thinning of the bilayer membrane and orientational disordering of lipid tails. Ethanol resides at the head-tail region of the membrane and enhances bilayer permeability. We found an envelope-protein-mediated increase in the ordering of lipid tails. Our simulations also provide important insights into the orientation of the envelope protein in a model membrane environment. At approximately 25 mol. % of ethanol in the surrounding ethanol-water phase, we observe disintegration of the lipid bilayer and dislocation of the E-protein from the membrane environment. Twit Text FOAVip The role of the envelope protein in the stability of a coronavirus model membrane against an ethanolic disinfectant ????J Chem Phys http://www.kidney.de/pget.php?&tw=1&pmid=34241335 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34241335 #FOAvip English Wikipedia <ref>{{Cite pmid|34241335}}</ref> The role of the envelope protein in the stability of a coronavirus model membrane against an ethanolic disinfectant #MMPMID34241335 Das S; Meinel MK; Wu Z; Muller-Plathe F J Chem Phys 2021[Jun]; 154 (24): 245101 PMID34241335show ga Ethanol is highly effective against various enveloped viruses and can disable the virus by disintegrating the protective envelope surrounding it. The interactions between the coronavirus envelope (E) protein and its membrane environment play key roles in the stability and function of the viral envelope. By using molecular dynamics simulation, we explore the underlying mechanism of ethanol-induced disruption of a model coronavirus membrane and, in detail, interactions of the E-protein and lipids. We model the membrane bilayer as N-palmitoyl-sphingomyelin and 1-palmitoyl-2-oleoylphosphatidylcholine lipids and the coronavirus E-protein. The study reveals that ethanol causes an increase in the lateral area of the bilayer along with thinning of the bilayer membrane and orientational disordering of lipid tails. Ethanol resides at the head-tail region of the membrane and enhances bilayer permeability. We found an envelope-protein-mediated increase in the ordering of lipid tails. Our simulations also provide important insights into the orientation of the envelope protein in a model membrane environment. At approximately 25 mol. % of ethanol in the surrounding ethanol-water phase, we observe disintegration of the lipid bilayer and dislocation of the E-protein from the membrane environment. |Cell Membrane/*drug effects/*metabolism[MESH] |Coronavirus/*metabolism/physiology[MESH] |Disinfectants/*pharmacology[MESH] |Ethanol/*pharmacology[MESH] |Lipid Bilayers/metabolism[MESH] |Molecular Conformation[MESH] |Molecular Dynamics Simulation[MESH] |Permeability[MESH]The role of the envelope protein in the stability of a coronavirus mod(epmc).pdf DeepDyve Pubget Overpricing