A quadtree-polygon-based scaled boundary finite element method for image-based mesoscale fracture modelling in concrete

A quadtree-polygon scaled boundary finite element-based approach for image-based modelling of concrete fracture at the mesoscale is developed. Digital images representing the two-phase mesostructure of concrete, which comprises of coarse aggregates and mortar are either generated using a take-and-place algorithm with a user-defined aggregate volume ratio or obtained from X-ray computed tomography as an input. The digital images are automatically discretised for analysis by applying a balanced quadtree decomposition in combination with a smoothing operation. The scaled boundary finite element method is applied to model the constituents in the concrete mesostructure. A quadtree formulation within the framework of the scaled boundary finite element method is advantageous in that the displacement compatibility between the cells are automatically preserved even in the presence of hanging nodes. Moreover, the geometric flexibility of the scaled boundary finite element method facilitates the use of arbitrary sided polygons, allowing better representation of the aggregate boundaries. The computational burden is significantly reduced as there are only finite number of cell types in a balanced quadtree mesh. The cells in the mesh are connected to each other using cohesive interface elements with appropriate softening laws to model the fracture of the mesostructure. Parametric studies are carried out on concrete specimens subjected to uniaxial tension to investigate the effects of various parameters e.g. aggregate size distribution, porosity and aggregate volume ratio on the fracture of concrete at the meso-scale. Mesoscale fracture of concrete specimens obtained from X-ray computed tomography scans are carried out to demonstrate its feasibility

Noncanonical and reversible cysteine ubiquitination prevents the overubiquitination of PEX5 at the peroxisomal membrane

PEX5, the peroxisomal protein shuttling receptor, binds newly synthesized proteins in the cytosol and transports them to the organelle. During its stay at the peroxisomal protein translocon, PEX5 is monoubiquitinated at its cysteine 11 residue, a mandatory modification for its subsequent ATP-dependent extraction back into the cytosol. The reason why a cysteine and not a lysine residue is the ubiquitin acceptor is unknown. Using an established rat liver-based cell-free in vitro system, we found that, in contrast to wild-type PEX5, a PEX5 protein possessing a lysine at position 11 is polyubiquitinated at the peroxisomal membrane, a modification that negatively interferes with the extraction process. Wild-type PEX5 cannot retain a polyubiquitin chain because ubiquitination at cysteine 11 is a reversible reaction, with the E2-mediated deubiquitination step presenting faster kinetics than PEX5 polyubiquitination. We propose that the reversible nonconventional ubiquitination of PEX5 ensures that neither the peroxisomal protein translocon becomes obstructed with polyubiquitinated PEX5 nor is PEX5 targeted for proteasomal degradation