Comparison of the aquatic toxicity of diquat and its metabolites to zebrafish Danio rerio.

Diquat (DQ) is a non-selective, fast-acting herbicide that is extensively used in aquatic systems. DQ has been registered as the substitute for paraquat due to its lower toxicity. However, the widespread presence of DQ in aquatic systems can pose an ecological burden on aquatic organisms.

Cross-Linked Polyacrylic-Based Hydrogel Polymer Electrolytes for Flexible Supercapacitors.

Hydrogel polymer electrolytes (GPEs), as an important component of flexible energy storage devices, have gradually received wide attention compared with traditional liquid electrolytes due to their advantages of good mechanical, bending, and safety properties. In this paper, two cross-linked GPEs of poly(acrylic acid-co-acrylamide) or poly(acrylic acid-co-N-methylolacrylamide) with NaNO aqueous solution (P(AA-co-AM)/NaNO or P(AA-co-HAM)/NaNO) were successfully prepared using radical polymerization, respectively, using acrylic acid (AA) as the monomer, N-methylolacrylamide (HAM) or acrylamide (AM) as the comonomer, and N, N-methylenebisacrylamide (MBAA) as the cross-linking agent. We investigated the morphology, glass transition temperature (), ionic conductivities, mechanical properties, and thermal stabilities of the two GPEs.

Emotional wellbeing in intercity travel: Factors affecting passengers' long-distance travel moods.

The travel mood perception can significantly affect passengers' mental health and their overall emotional wellbeing when taking transport services, especially in long-distance intercity travels. To explore the key factors influencing intercity travel moods, a field survey was conducted in Xi'an to collect passengers' individual habits, travel characteristics, moods, and weather conditions. Travel mood was defined using the 5-Likert scale, based on degrees of happiness, panic, anxiety, and tiredness.

Evaluating the Functional Pore Size of Chloroplast TOC and TIC Protein Translocons: Import of Folded Proteins.

The degree of residual structure retained by proteins while passing through biological membranes is a fundamental mechanistic question of protein translocation. Proteins are generally thought to be unfolded while transported through canonical proteinaceous translocons, including the translocons of the outer and inner chloroplast envelope membranes (TOC and TIC). Here, we readdressed the issue and found that the TOC/TIC translocons accommodated the tightly folded dihydrofolate reductase (DHFR) protein in complex with its stabilizing ligand, methotrexate (MTX).

New isoforms and assembly of glutamine synthetase in the leaf of wheat (Triticum aestivum L.).

Glutamine synthetase (GS; EC 6.3.1.

ATP requirement for chloroplast protein import is set by the Km for ATP hydrolysis of stromal Hsp70 in Physcomitrella patens.

The 70-kD family of heat shock proteins (Hsp70s) is involved in a number of seemingly disparate cellular functions, including folding of nascent proteins, breakup of misfolded protein aggregates, and translocation of proteins across membranes. They act through the binding and release of substrate proteins, accompanied by hydrolysis of ATP. Chloroplast stromal Hsp70 plays a crucial role in the import of proteins into plastids.

Energetic cost of protein import across the envelope membranes of chloroplasts.

Chloroplasts are the organelles of green plants in which light energy is transduced into chemical energy, forming ATP and reduced carbon compounds upon which all life depends. The expenditure of this energy is one of the central issues of cellular metabolism. Chloroplasts contain ~3,000 proteins, among which less than 100 are typically encoded in the plastid genome.

The chloroplast protein import system: from algae to trees.

Chloroplasts are essential organelles in the cells of plants and algae. The functions of these specialized plastids are largely dependent on the ~3000 proteins residing in the organelle. Although chloroplasts are capable of a limited amount of semiautonomous protein synthesis - their genomes encode ~100 proteins - they must import more than 95% of their proteins after synthesis in the cytosol.

The motors of protein import into chloroplasts.

Chloroplast function is largely dependent on its resident proteins, most of which are encoded by the nuclear genome and are synthesized in cytosol. Almost all of these are imported through the translocons located in the outer and inner chloroplast envelope membranes. The motor protein that provides the driving force for protein import has been proposed to be Hsp93, a member of the Hsp100 family of chaperones residing in the stroma.

Photosystem II, a growing complex: updates on newly discovered components and low molecular mass proteins.

Photosystem II is a unique complex capable of absorbing light and splitting water. The complex has been thoroughly studied and to date there are more than 40 proteins identified, which bind to the complex either stably or transiently. Another special feature of this complex is the unusually high content of low molecular mass proteins that represent more than half of the proteins.

A stromal heat shock protein 70 system functions in protein import into chloroplasts in the moss Physcomitrella patens.

Heat shock protein 70s (Hsp70s) are encoded by a multigene family and are located in different cellular compartments. They have broad-ranging functions, including involvement in protein trafficking, prevention of protein aggregation, and assistance in protein folding. Hsp70s work together with their cochaperones, J domain proteins and nucleotide exchange factors (e.

The low molecular mass subunits of the photosynthetic supracomplex, photosystem II.

The photosystem II (PSII) complex is located in the thylakoid membrane of higher plants, algae and cyanobacteria and drives the water oxidation process of photosynthesis, which splits water into reducing equivalents and molecular oxygen by solar energy. Electron and X-ray crystallography analyses have revealed that the PSII core complex contains between 34 and 36 transmembrane alpha-helices, depending on the organism. Of these helices at least 12-14 are attributed to low molecular mass proteins.