Milestones: Boosting women in seafood and ending gender inequality

This year, on 8 March, International Women’s Day (IWD), seven women engaged in seafood communities and promoting gender equality, released an opinion piece titled ‘Boosting women in seafood and ending gender inequality’

Yemaya recommends: Community fisheries organizations of Cambodia: Sharing processes, results and lessons learned in the context of the implementation of the SSF guidelines

This booklet, authored by John Kurien and published by the Food and Agriculture Organization (FAO) of the United Nations, brings together important insights on community empowerment in the traditional fisheries in Cambodia gleaned through field work and consultations undertaken between 2012 and 2015

Gender: Where have all the women gone?

Sex-segregated employment data in the recently released State of World Fisheries and Aquaculture 2018 report points to the need for better and more standardised data collection

Gulf of Kutch Marine National Park and Marine Wildlife Sanctuary: A case study

pdf has 46p

IFISH5: connecting the dots

In June this year, the city of St. John’s in Newfoundland and Labrador, Canada, played host to the largest gathering of fishing, aquaculture and seafood-processing safety and health professionals: the Fifth International Fishing Industry Safety and Health Conference (IFISH 5), the only conference dedicated to improving safety and health in the fishing industry. Held from 10 to 13 June 2018 in the picturesque campus of St. John’s Memorial University, and blessed – contrary to gloomy weather forecasts – by a few days of unexpected sunshine between rainy ones, IFISH 5 explored the latest research on occupational safety and health; discussed current fisheries policy and regulations; and showcased best practices for keeping workers safe and healthy

Structure and conformation of the disulfide bond in dimeric lung surfactant peptides SP-B1–25 and SP-B8–25

AbstractRaman spectroscopy was used to determine the conformation of the disulfide linkage between cysteine residues in the homodimeric construct of the N-terminal alpha helical domain of surfactant protein B (dSP-B1–25). The conformation of the disulfide bond between cysteine residues in position 8 of the homodimer of dSP-B1–25 was compared with that of a truncated homodimer (dSP-B8–25) of the peptide having a disulfide linkage at the same position in the alpha helix. Temperature-dependent Raman spectra of the S–S stretching region centered at ∼500 cm−1 indicated a stable, although highly strained disulfide conformation with a χ(CS–SC) dihedral angle of ±10° for the dSP-B1–25 dimer. In contrast, the truncated dimer dSP-B8–25 exhibited a series of disulfide conformations with the χ(CS–SC) dihedral angle taking on values of either ±30° or 85±20°. For conformations with χ(CS–SC) close to the ±90° value, the Raman spectra of the 8–25 truncated dimers exhibited χ(SS–CC) dihedral angles of 90/180° and 20–30°. In the presence of a lipid mixture, both constructs showed a ν(S–S) band at ∼488 cm−1, corresponding to a χ(CS–SC) dihedral angle of ±10°. Polarized infrared spectroscopy was also used to determine the orientation of the helix and β-sheet portion of both synthetic peptides. These calculations indicated that the helix was oriented primarily in the plane of the surface, at an angle of ∼60–70° to the surface normal, while the β structure had ∼40° tilt. This orientation direction did not change in the presence of a lipid mixture or with temperature. These observations suggest that: (i) the conformational flexibility of the disulfide linkage is dependent on the amino acid residues that flank the cysteine disulfide bond, and (ii) in both constructs, the presence of a lipid matrix locks the disulfide bond into a preferred conformation