Numerical Study of the Detonation Structure in Rich Acetylene-Air Mixtures

A numerical simulation of the detonation propagation process of acetylene-air under fuel-rich conditions is carried out using a reduced acetylene reaction model. The loose coupling method is used to solve the conservation equations with source terms. The flow is solved explicitly using a gas kinetic scheme, and the chemical reactions are solved implicitly. The numerical results show that the oxidation reaction is the chain initiation in the self-sustained detonation propagation process in rich acetylene. The self-decomposition reaction of acetylene provides the energy to maintain the coupling between the shock wave and the chemical reaction zone. The results show that the initial induced reaction is still an oxidation reaction due to the low activation energy of the oxidation reaction under the condition of low oxygen content. The intensity of the transverse wave is affected by the acetylene concentration. The post-detonation disturbance of temperature is mainly affected by the strength of the tail of transverse wave and the area of the unreacted pocket. With the increase of acetylene concentration, the self-decomposition process of acetylene increases the intensity of the transverse wave tail and improves the degree of temperature homogenization. This creates a formation-fragmentation-regeneration cycle of polycyclic aromatic hydrocarbons. This process changed the branching ratio of polycyclic aromatic hydrocarbons with different structures and delayed the formation of polycyclic aromatic hydrocarbons. When the acetylene concentration is low, the region where the dominant temperature after detonation is 1500 ~ 2500 K provides a favorable environment for the growth of polycyclic aromatic hydrocarbons.</p

Co-assembly of Amphiphilic Triblock Copolymers with Nanodrugs and Drug Release Kinetics in Solution

Polymeric vesicles present great potential in disease treatment as they can be featured as a structurally stable and easily functionalized drug carrier that can simultaneously encapsulate multiple drugs and release them on-demand. Based on the dissipative particle dynamics (DPD) simulation, the drug-loaded vesicles were designed by the co-assembly process of linear amphiphilic triblock copolymers and hydrophobic nanodrugs in solvents, and most importantly, the drug release behavior of drug-loaded vesicles were intensively investigated. The drug-loaded aggregates, such as vesicles, spherical micelles, and disk-like micelles, were observed by varying the size and concentration of nanodrugs and the length of the hydrophobic block. The distribution of nanodrugs in the vesicles was intensively analyzed. As the size of the nanodrugs increases, the localization of nanodrugs change from being unable to fully wrap in the vesicle wall to the uniform distribution and finally to the aggregation in the vesicles at the fixed concentration of nanodrugs. The membrane thickness of the drug-loaded polymeric vesicle can be increased, and the nanodrugs localized closer to the center of the vesicle by increasing the length of the hydrophobic block. The nanodrugs will be released from vesicles by varying the interactions between the nanodrug and the solvent or the hydrophobic block and the solvent, respectively. We found that the release kinetics conforms to the first-order kinetic model, which can be used to fit the cumulative release rate of nanodrugs over time. The results showed that increasing the size of nanodrugs, the length of hydrophobic block, and the interaction parameters between the hydrophobic block and the solvent will slow down the release rate of the nanodrug and change the drug release process from monophasic to biphasic release model

Table_3_Phylogenetic and AlphaFold predicted structure analyses provide insights for A1 aspartic protease family classification in Arabidopsis.xlsx

Aspartic proteases are widely distributed in animals, plants, fungi and other organisms. In land plants, A1 aspartic protease family members have been implicated to play important and varied roles in growth, development and defense. Thus a robust classification of this family is important for understanding their gene function and evolution. However, current A1 family members in Arabidopsis are less well classified and need to be re-evaluated. In this paper, 70 A1 aspartic proteases in Arabidopsis are divided into four groups (group I-IV) based on phylogenetic and gene structure analyses of 1200 A1 aspartic proteases which are obtained from 12 Embryophyta species. Group I-III members are further classified into 2, 4 and 7 subgroups based on the AlphaFold predicted structures. Furthermore, unique insights of A1 aspartic proteases have been unraveled by AlphaFold predicted structures. For example, subgroup II-C members have a unique II-C specific motif in the C-extend domain, and subgroup IV is a Spermatophyta conserved group without canonical DTGS/DSGT active sites. These results prove that AlphaFold combining phylogenetic analysis is a promising solution for complex gene family classification.</p

Image_9_Phylogenetic and AlphaFold predicted structure analyses provide insights for A1 aspartic protease family classification in Arabidopsis.tif

Aspartic proteases are widely distributed in animals, plants, fungi and other organisms. In land plants, A1 aspartic protease family members have been implicated to play important and varied roles in growth, development and defense. Thus a robust classification of this family is important for understanding their gene function and evolution. However, current A1 family members in Arabidopsis are less well classified and need to be re-evaluated. In this paper, 70 A1 aspartic proteases in Arabidopsis are divided into four groups (group I-IV) based on phylogenetic and gene structure analyses of 1200 A1 aspartic proteases which are obtained from 12 Embryophyta species. Group I-III members are further classified into 2, 4 and 7 subgroups based on the AlphaFold predicted structures. Furthermore, unique insights of A1 aspartic proteases have been unraveled by AlphaFold predicted structures. For example, subgroup II-C members have a unique II-C specific motif in the C-extend domain, and subgroup IV is a Spermatophyta conserved group without canonical DTGS/DSGT active sites. These results prove that AlphaFold combining phylogenetic analysis is a promising solution for complex gene family classification.</p

Table_1_Phylogenetic and AlphaFold predicted structure analyses provide insights for A1 aspartic protease family classification in Arabidopsis.xls

Aspartic proteases are widely distributed in animals, plants, fungi and other organisms. In land plants, A1 aspartic protease family members have been implicated to play important and varied roles in growth, development and defense. Thus a robust classification of this family is important for understanding their gene function and evolution. However, current A1 family members in Arabidopsis are less well classified and need to be re-evaluated. In this paper, 70 A1 aspartic proteases in Arabidopsis are divided into four groups (group I-IV) based on phylogenetic and gene structure analyses of 1200 A1 aspartic proteases which are obtained from 12 Embryophyta species. Group I-III members are further classified into 2, 4 and 7 subgroups based on the AlphaFold predicted structures. Furthermore, unique insights of A1 aspartic proteases have been unraveled by AlphaFold predicted structures. For example, subgroup II-C members have a unique II-C specific motif in the C-extend domain, and subgroup IV is a Spermatophyta conserved group without canonical DTGS/DSGT active sites. These results prove that AlphaFold combining phylogenetic analysis is a promising solution for complex gene family classification.</p

Co-assembly of Amphiphilic Triblock Copolymers with Nanodrugs and Drug Release Kinetics in Solution

Polymeric vesicles present great potential in disease treatment as they can be featured as a structurally stable and easily functionalized drug carrier that can simultaneously encapsulate multiple drugs and release them on-demand. Based on the dissipative particle dynamics (DPD) simulation, the drug-loaded vesicles were designed by the co-assembly process of linear amphiphilic triblock copolymers and hydrophobic nanodrugs in solvents, and most importantly, the drug release behavior of drug-loaded vesicles were intensively investigated. The drug-loaded aggregates, such as vesicles, spherical micelles, and disk-like micelles, were observed by varying the size and concentration of nanodrugs and the length of the hydrophobic block. The distribution of nanodrugs in the vesicles was intensively analyzed. As the size of the nanodrugs increases, the localization of nanodrugs change from being unable to fully wrap in the vesicle wall to the uniform distribution and finally to the aggregation in the vesicles at the fixed concentration of nanodrugs. The membrane thickness of the drug-loaded polymeric vesicle can be increased, and the nanodrugs localized closer to the center of the vesicle by increasing the length of the hydrophobic block. The nanodrugs will be released from vesicles by varying the interactions between the nanodrug and the solvent or the hydrophobic block and the solvent, respectively. We found that the release kinetics conforms to the first-order kinetic model, which can be used to fit the cumulative release rate of nanodrugs over time. The results showed that increasing the size of nanodrugs, the length of hydrophobic block, and the interaction parameters between the hydrophobic block and the solvent will slow down the release rate of the nanodrug and change the drug release process from monophasic to biphasic release model

Image_7_Phylogenetic and AlphaFold predicted structure analyses provide insights for A1 aspartic protease family classification in Arabidopsis.tif

Aspartic proteases are widely distributed in animals, plants, fungi and other organisms. In land plants, A1 aspartic protease family members have been implicated to play important and varied roles in growth, development and defense. Thus a robust classification of this family is important for understanding their gene function and evolution. However, current A1 family members in Arabidopsis are less well classified and need to be re-evaluated. In this paper, 70 A1 aspartic proteases in Arabidopsis are divided into four groups (group I-IV) based on phylogenetic and gene structure analyses of 1200 A1 aspartic proteases which are obtained from 12 Embryophyta species. Group I-III members are further classified into 2, 4 and 7 subgroups based on the AlphaFold predicted structures. Furthermore, unique insights of A1 aspartic proteases have been unraveled by AlphaFold predicted structures. For example, subgroup II-C members have a unique II-C specific motif in the C-extend domain, and subgroup IV is a Spermatophyta conserved group without canonical DTGS/DSGT active sites. These results prove that AlphaFold combining phylogenetic analysis is a promising solution for complex gene family classification.</p

Image_6_Phylogenetic and AlphaFold predicted structure analyses provide insights for A1 aspartic protease family classification in Arabidopsis.tif

Aspartic proteases are widely distributed in animals, plants, fungi and other organisms. In land plants, A1 aspartic protease family members have been implicated to play important and varied roles in growth, development and defense. Thus a robust classification of this family is important for understanding their gene function and evolution. However, current A1 family members in Arabidopsis are less well classified and need to be re-evaluated. In this paper, 70 A1 aspartic proteases in Arabidopsis are divided into four groups (group I-IV) based on phylogenetic and gene structure analyses of 1200 A1 aspartic proteases which are obtained from 12 Embryophyta species. Group I-III members are further classified into 2, 4 and 7 subgroups based on the AlphaFold predicted structures. Furthermore, unique insights of A1 aspartic proteases have been unraveled by AlphaFold predicted structures. For example, subgroup II-C members have a unique II-C specific motif in the C-extend domain, and subgroup IV is a Spermatophyta conserved group without canonical DTGS/DSGT active sites. These results prove that AlphaFold combining phylogenetic analysis is a promising solution for complex gene family classification.</p

Image_1_Phylogenetic and AlphaFold predicted structure analyses provide insights for A1 aspartic protease family classification in Arabidopsis.tif

Aspartic proteases are widely distributed in animals, plants, fungi and other organisms. In land plants, A1 aspartic protease family members have been implicated to play important and varied roles in growth, development and defense. Thus a robust classification of this family is important for understanding their gene function and evolution. However, current A1 family members in Arabidopsis are less well classified and need to be re-evaluated. In this paper, 70 A1 aspartic proteases in Arabidopsis are divided into four groups (group I-IV) based on phylogenetic and gene structure analyses of 1200 A1 aspartic proteases which are obtained from 12 Embryophyta species. Group I-III members are further classified into 2, 4 and 7 subgroups based on the AlphaFold predicted structures. Furthermore, unique insights of A1 aspartic proteases have been unraveled by AlphaFold predicted structures. For example, subgroup II-C members have a unique II-C specific motif in the C-extend domain, and subgroup IV is a Spermatophyta conserved group without canonical DTGS/DSGT active sites. These results prove that AlphaFold combining phylogenetic analysis is a promising solution for complex gene family classification.</p

DataSheet_1_Phylogenetic and AlphaFold predicted structure analyses provide insights for A1 aspartic protease family classification in Arabidopsis.pdf

Aspartic proteases are widely distributed in animals, plants, fungi and other organisms. In land plants, A1 aspartic protease family members have been implicated to play important and varied roles in growth, development and defense. Thus a robust classification of this family is important for understanding their gene function and evolution. However, current A1 family members in Arabidopsis are less well classified and need to be re-evaluated. In this paper, 70 A1 aspartic proteases in Arabidopsis are divided into four groups (group I-IV) based on phylogenetic and gene structure analyses of 1200 A1 aspartic proteases which are obtained from 12 Embryophyta species. Group I-III members are further classified into 2, 4 and 7 subgroups based on the AlphaFold predicted structures. Furthermore, unique insights of A1 aspartic proteases have been unraveled by AlphaFold predicted structures. For example, subgroup II-C members have a unique II-C specific motif in the C-extend domain, and subgroup IV is a Spermatophyta conserved group without canonical DTGS/DSGT active sites. These results prove that AlphaFold combining phylogenetic analysis is a promising solution for complex gene family classification.</p