Amorpha-4,11-diene synthase (ADS) is the first committed enzyme in the biosynthesis of artemisinin. Artemisinin production by biobased fermentation is considered a reliable alternative pathway. Heterologously expressed ADS has been established to generate several minor products, including structural analogues of amorpha-4,11-diene, but their fate in fermentation is still unknown. Here, using chiral analysis, we found that ADS produces one of the analogues, amorpha-4-en-11-ol, as a pair of epimers. Labeling experiments revealed that ADS mutants yielded amorphene-type sesquiterpenes, indicating the co-occurrence of initial 1,6 and 1,10 cyclization of farnesyl diphosphate in a single enzyme. Interestingly, the immediate downstream oxidase CYP71AV1 had very low affinity to the side products of the recombinant ADS, including amorpha-4-en-7-ol, which is structurally similar to amorpha-4,11-diene. Our data uncover the complex catalytic mechanism of recombinant ADS and reveal a potential negative effect of the side products of recombinant ADS on the production of the artemisinin precursor in microbes.Mechanical properties of aerogels are controlled by the connectivity of their network. In this paper, in order to study these properties, computational models of silica aerogels with different morphological entities have been generated by means of the diffusion-limited cluster-cluster aggregation (DLCA) algorithm. New insights into the influence of the model parameters on the generated aerogel structures and on the finite deformation under mechanical loads are provided. First, the structural and fractal properties of the modeled aerogels are investigated. The dependence of morphological properties such as the particle radius and density on these properties is studied. The results are correlated with experimental small-angle X-ray scattering (SAXS) data of a silica aerogel. The DLCA models of silica aerogels are analyzed for their mechanical properties with finite element simulations. There, the aerogel particles are modeled as nodes and the interparticle bonds as beam elements to account for bond stretching, bending, and torsion. The scaling relation between the elastic moduli E and relative density ρ, E ∝ ρ m , is investigated and the exponent m = 3.61 is determined. Backbone paths evidently appear in the 3-d network structure under deformation, while the majority of the bonds in the network do not bear loads. The sensitivity of particle neck-sizes on the mechanical properties is also studied. All the results are shown to be qualitatively as well as quantitatively in agreement with the experimental data or with the available literature.As part of the United States Environmental Protection Agency’s 2010 Nitrogen Dioxide (NO2) National Ambient Air Quality Standards (NAAQS) review, a national network of near-road sites was established to characterize pollutant behavior, interaction, and dispersion in the ambient near-road environment. Using spatial interpolation to estimate the near-road concentration increments of NO2 and particulate matter with an aerodynamic diameter of 2.5 μm and less (PM2.5) relative to nearby non-near-road monitors, we found that the 2013-2018 national average increment is 6.9 ppb and 1.0 μg m-3 for NO2 and PM2.5, respectively. Analyses of the hourly near-road NO2, nitric oxide (NO), and PM2.5 increments showed distinct diurnal cycles; the NO2 increment peaks at ∼9 ppb during the early afternoon (2-4 pm local time) while the NO and PM2.5 increments peak during the morning rush hour (5-8 am local time) at 25 ppb and 1.8 μg m-3 for NO and PM2.5, respectively. Although long-term trends are not yet available for this network of sites, a similar analysis of the NO2 and PM2.5 increment at a quasi-near-road site outside of the official network in Elizabeth, NJ showed gradual decreases in the increment over time since the mid-2000s.Is there a criterion able to determine the type of structures formed in a nonequilibrium self-assembly process? This important question has a clear answer when the process takes place under equilibrium conditions structures emerge at minimum values of the free energy. read more Experiments, however, have shown that when self-assembly takes place outside equilibrium, they do not appear at those free energy minima but rather at optimal values of structural parameters. On the basis of these observations, we propose a selection criterion for which structures come up at the minima of a nonequilibrium free energy that takes into account the energy needed to change their configuration. The criterion is able to predict the formation and configuration of structures such as Liesegang rings and patterns in magnetic colloids and could constitute a powerful tool to understand the synthesis of advanced materials, enantiomers, and nanoparticles.Human γD (HγD) and γC (HγC) are two-domain crystallin (Crys) proteins expressed in the nucleus of the eye lens. Structural perturbations in the protein often trigger aggregation, which eventually leads to cataract. To decipher the underlying molecular mechanism, it is important to characterize the partially unfolded conformations, which are aggregation-prone. Using a coarse grained protein model and molecular dynamics simulations, we studied the role of on-pathway folding intermediates in the early stages of aggregation. The multidimensional free energy surface revealed at least three different folding pathways with the population of partially structured intermediates. The two dominant pathways confirm sequential folding of the N-terminal [Ntd] and the C-terminal domains [Ctd], while the third, least favored, pathway involves intermediates where both the domains are partially folded. A native-like intermediate (I*), featuring the folded domains and disrupted interdomain contacts, gets populated in all three pathways. I* forms domain swapped dimers by swapping the entire Ntds and Ctds with other monomers. Population of such oligomers can explain the increased resistance to unfolding resulting in hysteresis observed in the folding experiments of HγD Crys. An ensemble of double domain swapped dimers are also formed during refolding, where intermediates consisting of partially folded Ntds and Ctds swap secondary structures with other monomers. The double domain swapping model presented in our study provides structural insights into the early events of aggregation in Crys proteins and identifies the key secondary structural swapping elements, where introducing mutations will aid in regulating the overall aggregation propensity.