Assessment of brain injury biomechanics in soccer heading using finite element analysis

This study presents an in silico finite element (FE) model-based biomechanical analysis of brain injury metrics and associated risks of a soccer ball impact to the head for aware and unaware athletes, considering ball impact velocity and direction. The analysis presented herein implements a validated soccer ball and 50th percentile human head computational FE model for quantifying traumatic brain injury (TBI) metrics. The brain's mechanical properties are designated using a viscoelastic-viscoplastic constitutive material model for the white and gray matter within the human head FE model. FE results show a dynamic human head-soccer ball peak contact area of approximately seven times greater than those documented for helmet-to-helmet hits in American Football. Due to the deformable nature of the soccer ball, the impact dynamics are unique depending on the location and velocity of impact. TBI injury risks also depend on the location of impact and the impact velocity. Impacts to the rear (BrIC:0.48, HIC15:180.7), side (BrIC:0.52, HIC15:176.5), and front (BrIC:0.37, HIC15:129.0) are associated with the highest injury risks. Furthermore, the FE results indicate when an athlete is aware of an incoming ball, HIC15-based Abbreviated Injury Scale 1 (AIS 1) injury risks for the front, side, and rear impacts decrease from 10.5%, 18.5%, and 19.3%, respectively, to approximately 1% in front and side impacts and under 6% in a rear impact. Lastly, the unique contact area between the head and soccer ball produces pressure gradients in the ball that translate into distinguishable stress waves in the skull and the cerebral cortex

Active site analysis of yeast flavohemoglobin based on its structure with a small ligand or econazole

Flavohemoglobins (flavoHbs) serve various microorganisms as the major protective enzymes against NO˙-mediated toxicity. FlavoHbs dominantly function as an NO˙ dioxygenase (O2 + NO → NO3-), the required electron being shuttled from NAD(P)H via FAD to the heme iron. The X-ray structures of the flavoHb from Saccharomyces cerevisae presented in complex with an unknown small ligand (Yhb) and with econazole (YhbE) at 2.1 and 3.0 Å resolutions, respectively, reveal a high architectural accordance between prokaryotic and eukaryotic family members. The active site is characterized by a proximal heme side with a strictly conserved histidine, glutamate and tyrosine triad and a highly variable distal heme side with helix shifts up to 10 Å mainly dependent on the presence/absence and size of the bound ligand. In yeast flavoHb, the small heme iron ligand adjusts a catalytically productive active site geometry that reliably suggests the NO and O2 binding site. O2 is activated by its ligation to an electron-rich heme iron and a hydrogen bond to Tyr29 and Gln53. High active site similarities between eukaryotic Yhb and bacterial single-domain globins argue for identical biochemical reactions. Binding of the bulky econazole implies a large-scale induced-fit process concerning, in particular, an outwards shift of helices B and E to increase the active site pocket. Yeast Yhb and Ralstonia eutropha flavoHb both structurally studied in complex with econazole indicate conformational differences between the inhibitors and the polypeptide primarily caused by stable binding of a phospholipid to the latter and by distinct loop D structures