No abstract

Ni/NiO core-shell nanowires on nickel foam (NF) are successfully synthesized using an "acid-hungry" strategy. The 3D electrode with large accessible active sites and improved conductivity, possesses an optimized ionic and electronic transport path during electrochemical processes. High areal capacitance of 1.65 F cm is obtained at an ultrahigh current density of 100 mA cm , which is 19.88 times higher than pristine NF. The direct growth of nanowires makes the present supercapacitor electrode robust for long-term cycling test. By virtue of the favorable hydrogen adsorption energies on Ni and OH energy on NiO or NiOOH, the 3D electrode exhibits high performance in hydrogen evolution reaction with 146 mV at η10 mA cm-2 and Tafel value of 72 mV dec , and oxygen evolution reaction with 382 mV at η10 mA cm-2 and Tafel value of 103 mV dec in 1 m KOH. An electrolyzer using 3D electrodes as both anode and cathode can yield a current density of 10 mA cm at 1.71 V, and possesses superior long-term stability to an electrolyzer consisting of Pt/C||Ir/C. The present work develops an effective and low-cost method for the large-scale fabrication of Ni/NiO core-shell nanowires on commercial NF, providing a promising candidate for supercapacitors, fuel cells, and electrocatalysis.

To better appreciate the alterations of egg proteins and their modifications during embryonic development, a comparative and quantitative study was performed aimed at chicken egg white and yolk proteome and N-glycoproteome after 12 days of incubation using tandem mass tag (TMT)-labeling technology in conjunction with reversed-phase high-performance liquid chromatography (RP-HPLC). A total of 334 unique N-glycosite-containing peptides from 153 N-glycoproteins were identified, of which 82 N-glycosite-containing peptides showed significant changes after 12 days of incubation. The varied proteome was mainly involved with antibacterial, ionic binding, cell proliferation, and embryonic development, while the different degrading and/or absorbing priorities of egg proteins were proposed. This study provides substantial insight into the effects of N-glycoprotein variations on the utilization of egg proteins by chicken embryo during incubation.

Protein phosphorylation plays an important role in protein structure and function. To investigate the role of egg protein phosphorylation in chicken embryonic development, a comparative and quantitative phosphoproteomic analysis of fertilized chicken egg white and yolk was performed during incubation. Overall, 215 phosphosites mapped onto 205 phosphopeptides corresponding to 100 phosphoproteins were identified. Among these phosphoproteins, 123 phosphosites from 62 egg proteins were found significantly changed (p < 0.05) at day 12 during incubation. Furthermore, GO analysis suggested that these differentially phosphorylated proteins were associated with various molecular functions, primarily including binding, molecular function regulator, and transport activity. Such findings in this study improved our understanding of the protein molecular functions involved in chicken embryonic development from a protein phosphorylation perspective.

Searching for promising HER electrocatalysts is an urgent task for the practical application of hydrogen production by water electrolysis.