- The study focuses on the N-terminal fragment of the influenza A hemagglutinin (HA) HA2 subunit, specifically a fusion peptide (HAfp), highlighting the significance of its C-terminal residues (W21-Y22-G23) in structural formation and stability.
- Researchers investigated how varying the length of the fusion peptide affects its fusion properties, structure, and interaction with membranes, utilizing a fusion visualization assay and molecular dynamics simulations.
- Findings indicate that the longer HAfp promotes a distinct helical hairpin structure which enhances lipid disorder and leads to the formation of cholesterol-enriched domains, unlike the shorter variant (HAfp1-20).
At a major vascular surgery center, foundation year one doctors often struggle to meet national record-keeping standards when documenting patient admissions, which poses risks to patient safety.
A literature review highlighted that high-quality clerkings enhance patient safety and suggested using a pro forma to improve documentation compliance.
After introducing a clerking pro forma based on national guidelines, documentation quality significantly improved across various areas, suggesting enhanced patient safety and a recommendation for wider implementation in the hospital.