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Keratins are considered ideal candidates as hemostatic agents, but the development lags far behind their potentials due to the poorly understood hemostatic mechanism and structure-function relations, owing to the composition complexity in protein extracts. Here, it is shown that by using a recombinant synthesis approach, individual types of keratins can be expressed and used for mechanism investigation and further high-performance keratin hemostatic agent design. In the comparative evaluation of full-length, rod-domain, and helical segment keratins, the 𝜶-helical contents in the sequences are identified to be directly proportional to keratins' hemostatic activities, and Tyr, Phe, and Gln residues at the N-termini of 𝜶-helices in keratins are crucial in fibrinopeptide release and fibrin polymerization. A feasible route to significantly enhance the hemostatic efficiency of helical keratins by mutating Cys to Ser in the sequences for enhanced water wettability through soluble expression is then further presented. These results provide a rational strategy to design high-efficiency keratin hemostatic agents with superior performance over clinically used gelatin sponge in multiple animal models.

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The grounding grid buried in the earth will become a hidden danger to the safety of substations due to some faults of breaks or thinner conductors in corrosion. A novel method to get accurate status of grounding grid was proposed based on measuring magnetic induction intensity. The basic structure of grounding grid without working drawing was concluded, and the positions and the status of faults were diagnosed by this method. The completed detecting system, including hardware device of data measurement, diagnosis, and analysis software, was introduced concisely. The results of simulations and applications show that this method is simple and effective in the practical engineering.

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Insect Odorant-Binding Proteins (OBPs) play crucial roles in the discrimination, binding and transportation of odorants. Herein, the full-length cDNA sequence of Minus-C OBP1 (MaltOBP1) from the Japanese pine sawyer beetle, Monochamus alternatus, was cloned by 3 and 5 RACE-PCR and analyzed. The results showed that MaltOBP1 contains a 435 bp open reading frame (ORF) that encodes 144 amino acids, including a 21amino acid signal peptide at the N-terminus. The matured MaltOBP1 protein possesses a predicted molecular weight of about 14 kDa and consists of six α-helices, creating an open binding pocket, and two disulfide bridges. Immunoblotting results showed that MaltOBP1 was most highly expressed in antennae in both sexes, followed by wings and legs. Fluorescence assays demonstrated that MaltOBP1 protein exhibited high binding affinity with (R)-(+)-α-pinene, (−)-β-pinene, trans-caryophyllene, (R)-(+)-limonene and (-)-verbenone, which are the main volatile compounds of the pine tree. Our combined results suggest that MaltOBP1 plays a role in host seeking behavior in M. alternatus.