Procalcitonin (PCT), a member of the calcitonin (CT) superfamily, is a 116 amino acid, 13 kilodalton precursor protein produced in humans in the parafollicular cells of the thyroid as well as the neuroendocrine cells of the lungs and intestines of healthy individuals. PCT is coded for in the Calc‐I gene, located on chromosome 11. PCT is the precursor to the regulatory protein calcitonin but may have its own, separate role in the human body’s response to bacterial infection. There is a positive correlation between the concentration of PCT in the blood and the severity of a bacterial infection, making PCT an acute phase reactant. Under normal conditions, PCT undergoes proteolytic cleavage in the thyroid and is converted into CT, which then leaves the thyroid and enters the bloodstream; however, under inflammatory conditions, PCT is not cleaved and enters the bloodstream in a three‐section state comprising an amino terminus, immature calcitonin, and calcitonin carboxyl‐terminus peptide. Additionally, under inflammatory conditions, PCT is produced in other locations besides the parafollicular cells of the thyroid and the neuroendocrine cells of the lungs and intestines due to an increase in the expression of the Calc‐I gene. The reason for this increase may be related to potential anti‐inflammatory characteristics of PCT, including an ability to signal a reduction in the production of pro‐inflammatory proteins such as tumor necrosis factor‐alpha and interleukin 1‐beta. Furthermore, PCT in a specific concentration has been shown to reduce the reactivity of lipopolysaccharide (LPS) in gram‐negative bacteria. These properties of PCT have many potential applications in the medical field that are currently being studied or used. For example, detection of PCT in the blood can be used to determine if an infection is viral or bacterial or to evaluate the severity of infection in patients with sepsis. The determination of the pathogen allows for the correct course of appropriate treatment, potentially preventing the overprescription and overuse of antibiotics, a critical concern with the continued rise of bacterial antibiotic resistance. Additionally, as patients recover from a systemic bacterial infection, monitoring the level of PCT allows physicians to determine when the course of antibiotics may be stopped, once again minimizing antibiotic overuse. The Walton High School SMART Team has designed a 3D model of procalcitonin to investigate the relationship between procalcitonin’s structure and its function. Support or Funding Information MSOE Center for Biomolecular Modeling

ATP8A1‐CDC50a is a Type 4 P‐type ATPase protein composed of two subunit proteins, the ATP8A1 section and the CDC50a section, connected by heterodimerization. Originally found in red blood cells, the ATP8A1 section was the first identified member of the P4‐ATPase family and works as a flippase that uses the energy from ATP hydrolysis to translocate phospholipids from the outer to inner leaflet of eukaryotic cellular membranes in order to maintain phospholipid asymmetry necessary for membrane trafficking, membrane biogenesis, apoptosis, and signaling pathways. CDC50 proteins are common binding partners of the human class‐1 P‐ATPases to form heteromeric complexes which, in the case of ATP8A1‐CDC50a, associate with and recruit P4‐ATPase ATP8A1 to the plasma membrane. The CDC50a section functions as a chaperone protein to ATP8A1 and facilitates the proper folding and flippase activity. Mutations in some P4‐ATPases cause inherited genetic diseases such as with ATP8A1‐CDC50a and ATP8A2‐CDC50, two closely related proteins in the P4‐ATPase family, which can cause neurological disorders and learning deficits; however, only ATP8A2‐CDC50 mutations are linked to severe neurological defects, whereas there is no clear disease associations linked to ATP8A1‐CDC50a. Despite this, overexpression of CDC50a leads to extensive cell spreading and enhanced cell migration while a deficiency of either CDC50A or ATP8A1 may lead to severe defects in the formation of membrane ruffles, in turn inhibiting cell migration. The Walton SMART team has designed a 3D model of ATP8A1‐CDC50a to investigate the relationship between its structure and function.