The new SARS-CoV-2 strain shows a stronger binding affinity to ACE2due to N501Y mutant

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

The New SARS-CoV-2 Strain Shows a Stronger Binding Affinity to ACE2 Due to N501Y Mutation

SARS-CoV-2 is a global challenge due to its ability to spread much faster than SARS-CoV, which was attributed to the mutations in the receptor binding domain (RBD). These mutations enhanced the electrostatic interactions. Recently, a new strain was reported in the UK that includes a mutation (N501Y) in the RBD, that possibly increases the infection rate. Using Molecular Dynamics simulations (MD) and Monte Carlo (MC) sampling, we showed that the N501 mutation enhances 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

Comparing the binding interactions in the receptor binding domains of SARS-CoV-2 and SARS-CoV

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

A unified global investigation on the spectral effects of soiling losses of PV glass substrates: preliminary results.

The present work reports on the initial results of an international collaboration aiming to investigate the spectral effects of soiling losses. Identical glass coupons have been exposed outdoors for eight weeks in different locations worldwide, and weekly direct and hemispherical transmittance (T%) measurements are compared. Maximum losses as high as 7% and 50% in hemispherical and direct transmittance, respectively, have been found during the 8-week outdoor exposure. At the end of the data collection, a preliminary analysis of the spectral impact of soiling has been performed. The results show that the blue end of the spectrum is more affected and that lower hemispherical T% correlate to larger area covered by particles

Modelling photovoltaic soiling losses through optical characterization

The accumulation of soiling on photovoltaic (PV) modules affects PV systems worldwide. Soiling consists of mineral dust, soot particles, aerosols, pollen, fungi and/or other contaminants that deposit on the surface of PV modules. Soiling absorbs, scatters, and reflects a fraction of the incoming sunlight, reducing the intensity that reaches the active part of the solar cell. Here, we report on the comparison of naturally accumulated soiling on coupons of PV glass soiled at seven locations worldwide. The spectral hemispherical transmittance was measured. It was found that natural soiling disproportionately impacts the blue and ultraviolet (UV) portions of the spectrum compared to the visible and infrared (IR). Also, the general shape of the transmittance spectra was similar at all the studied sites and could adequately be described by a modified form of the Ångström turbidity equation. In addition, the distribution of particles sizes was found to follow the IEST-STD-CC 1246E cleanliness standard. The fractional coverage of the glass surface by particles could be determined directly or indirectly and, as expected, has a linear correlation with the transmittance. It thus becomes feasible to estimate the optical consequences of the soiling of PV modules from the particle size distribution and the cleanliness value

Comparing the binding interactions in the receptor binding domains of SARS-CoV-2 and SARS-CoV

SARS-CoV-2, since emerging in Wuhan, China, has been a major concern because of its high infection rate and has left more than six million infected people around the world. Many studies endeavored to reveal the structure of the SARS-CoV-2 compared to the SARS-CoV, in order to find solutions to suppress this high infection rate. Some of these studies showed that the mutations in the SARS-CoV spike (S) 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 S proteins of SARS-CoV and SARS-CoV-2 to the ACE2. Our results show that the protein surface of the ACE2 at the receptor binding domain (RBD) exhibits negative electrostatic potential, while a positive potential is observed for the S proteins of SARS-CoV/SARS-CoV-2. In addition, the binding energies at the interface are slightly higher for SARS-CoV-2 because of enhanced electrostatic interactions. The major contributions to the electrostatic binding energies result from the salt bridges forming between R426 and ACE-2-E329 in the case of SARS-CoV and K417 and ACE2-D30 in the SARS-CoV-2. In addition, our results indicate that the enhancement in the binding energy is not due to a single mutant but rather because of the sophisticated structural changes induced by all these mutations together. This finding suggests that it is implausible for the SARS-CoV-2 to be a lab-engineered virus