Graphene is considered a leading candidate to replace conventional transparent conducting electrodes because of its high transparency and exceptional transport properties. The effect of chemical p-type doping on graphene stacks was studied in order to reduce the sheet resistance of graphene films to values approaching those of conventional transparent conducting oxides. In this report, we show that large-area, stacked graphene films are effectively p-doped with nitric acid. The doping decreases the sheet resistance by a factor of 3, yielding films comprising eight stacked layers with a sheet resistance of 90 Omega/(square) at a transmittance of 80%. The films were doped either after all of the layers were stacked (last-layer-doped) or after each layer was added (interlayer-doped). A theoretical model that accurately describes the stacked graphene film system as a resistor network was developed. The model defines a characteristic transfer length where all the channels in the graphene films actively contribute to electrical transport. The experimental data shows a linear increase in conductivity with the number of graphene layers, indicating that each layer provides an additional transport channel, in good agreement with the theoretical model.
COVID-19, since emerged in Wuhan, China, has been a major concern due to its high infection rate, leaving more than one million infected people around the world. Huge number of studies tried to reveal the structure of the SARS-CoV-2 compared to the SARS-CoV-1, in order to suppress this high infection rate. Some of these studies showed that the mutations in the SARS-CoV-1 Spike protein might be responsible for its higher affinity to the ACE2 human cell receptor. In this work, we used molecular dynamics simulations and Monte Carlo sampling to compare the binding affinities of the spike proteins of SARS-CoV and SARS-CoV-2 to the ACE2. We found that the SARS-CoV-2 binds to ACE2 stronger than SARS-CoV by 7 kcal/mol, due to enhanced electrostatic interactions. The major contributions to the electrostatic binding energies are resulting from the salt-bridges formed between R426 and ACE2-E329 in case of SARS-CoV and K417 and ACE2-D30 for SARS-CoV2. In addition, there is no significant contribution from a single mutant to the binding energies. However, these mutations induce sophisticated structural changes that enhance the binding energies. Our results also indicate that the SARS-CoV-2 is unlikely a lab engineered virus.
SARS-CoV-2 is a global challenge due to its ability to spread much faster than the SARS-CoV, which was attributed to the mutations in the receptor binding domain (RBD). These mutations enhanced the electrostatic interactions. Recently, a new strain is reported in the UK that includes a mutation (N501Y) in the RBD, that is possibly increasing the infection rate. Here, using Molecular Dynamics simulations (MD) and Monte Carlo (MC) sampling, we show that the N501 mutation enhanced the electrostatic interactions due to the formation of a strong hydrogen bond between SARS-CoV-2-T500 and ACE2-D355 near the mutation site. In addition, we observed that the electrostatic interactions between the SARS-CoV-2 and ACE2 in the wild type and the mutant are dominated by salt-bridges formed between SARS-CoV-2-K417 and ACE2-D30, SARS-CoV-2-K458, ACE2-E23, and SARS-CoV-2-R403 and ACE2-E37. These interactions contributed more than 40% of the total binding energies.
Fluorescence quenching is a powerful technique used to obtain information about the dynamic changes of proteins in complex macromolecular systems. In this work, graphene is shown to be a very efficient quencher of fluorescence molecules where the quenching effect was one order of magnitude higher than that of gold. The fluorescence intensity was distance-dependent where increasing the distance between the fluorescence molecule and the graphene surface from 4 to 7 nm increased the fluorescence intensity by a factor of 7.5. This type of distance dependence suggests a nonradiative nature in the energy transfer between the graphene and the fluorophore due to the excitation of an exciton.
A long range surface plasmon (LRSP) is an electromagnetic wave propagating along a thin metal film with an order of magnitude lower damping than conventional surface plasmon (SP) waves. Thus, the excitation of LRSP is associated with a narrower resonance and it provides larger enhancement of intensity of the electromagnetic field. In surface plasmon resonance (SPR) biosensors, these features allow a more precise observation of the binding of biomolecules in the proximity to the metal surface by using the (label-free) measurement of refractive index (RI) variations and by SP-enhanced fluorescence spectroscopy. In this contribution, we investigate LRSPs excited on a layer structure consisting of a fluoropolymer buffer layer, a thin gold film, and an aqueous sample. By implementing such structure in an SPR sensor, we achieved a 2.4-and 4.4-fold improvement of the resolution in the label-free and fluorescence-based detection, respectively, of the binding of biomolecules in the close proximity to the surface. Moreover, we demonstrate that the sensor resolution can be improved by a factor of 14 and 12 for the labelfree and fluorescence-based detection, respectively, if the biomolecular binding events occur within the whole evanescent field of LRSP.
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