https://www.selleckchem.com/products/adavivint.html The fusion of the viral and target cell membranes is a key step in the life cycle of all enveloped viruses. Here, a range of structural data is used to generate an evidence-based model of the active conformation of an archetypical type-I fusion protein, the Ebola glycoprotein 2 (GP2). The stability of the trimeric complex is demonstrated using molecular dynamics and validated by simulating the interaction of the complex with a lipid bilayer. In this model, the fusion peptides project away from the central helix bundle parallel to the target membrane. This maximizes contact with the host membrane, enhances lateral stability, and would explain why, when activated, viral fusion proteins are trimeric.To address the obstinate problem of the shuttle effect in lithium-sulfur (Li-S) batteries, cathode materials are usually given multifunctions to immobilize sulfur, which increases the processing difficulty of cathode materials and weakens the advantage in energy density of Li-S batteries. Herein, a single-source decomposition approach is employed to synthesize a pomegranate-like nitrogenous carbon-coated ZnS (ZnS@NC) precursor that is acid etched to obtain the partially etched ZnS@NC (PE-ZnS@NC) composite. PE-ZnS@NC is coated on a commercial PP separator to a fabricate PE-ZnS@NC/PP functional separator that is used to assemble a coin cell with the sulfur/super P cathode. The 3D network carbon framework of PE-ZnS@NC provides additional active sites for electrochemical reaction and a space barrier for the diffusion of the dissolved lithium polysulfides (LPS). Well-distributed N-containing functional groups and polar ZnS could chemically anchor LPS. Also, the ZnS nanoparticles inside could facilitate a fast kinetic process by catalyzing the liquid-liquid and liquid-solid conversion. Since the shuttle effect is greatly suppressed by the synergistic trifunctions of blockage-chemisorption catalysis, PE-ZnS@NC/PP delivers remarka