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Objectives Patients with chronic illnesses, including kidney disease, consider their sense of normalcy when evaluating their health. Although this concept is a key indicator of their self-determined well-being, they struggle to understand if their experience is typical. To address this challenge, we set out to explore how to design personal health visualizations that aid participants in better understanding their experiences post-transplant, identifying barriers to normalcy, and achieving their desired medical outcomes. Materials and Methods Pediatric kidney transplant patients and their caregivers participated in three asynchronous design sessions involving sharing experiences, presenting symbolic objects, and providing feedback on visualizations to understand their perceptions of normalcy post-transplant. Data analysis of design session 1 and 2 comprised deductive and inductive analysis. We used affinity diagramming to identify thematic areas about participants' transplant experiences. Comprehension of design session three normalcy visualizations was also evaluated. Results Participants effectively engaged in the design sessions, revealing diverse perspectives on their experiences. We found there is a significant need for visualizations that depict normalcy to better inform patients and caregivers about their health. Discussion Normalcy Visualizations should incorporate three key design principles: personal values, facilitating peer and self-comparison, and seamlessly communicating abstract concepts to help youth kidney transplant recipients comprehend and contextualize if their transplant experience is normal and what normalcy means to them. Conclusion By incorporating holistic aspects of patients' and caregivers' lives into personal health visualizations, they can be cognizant of their progress to normalcy and empowered to make decisions that help them feel normal. [ABSTRACT FROM AUTHOR]

The primary role of bacterial periplasmic binding proteins is sequestration of essential metabolites present at a low concentration in the periplasm and making them available for active transporters that transfer these ligands into the bacterial cell. The periplasmic binding proteins (SiaPs) from the tripartite ATP-independent periplasmic (TRAP) transport system that transports mammalian host-derived sialic acids have been well studied from different pathogenic bacteria, including Haemophilus influenzae, Fusobacterium nucleatum, Pasteurella multocida, and Vibrio cholerae. SiaPs bind the sialic acid N-acetylneuraminic acid (Neu5Ac) with nanomolar affinity by forming electrostatic and hydrogen-bonding interactions. Here, we report the crystal structure of a periplasmic binding protein (SatA) of the ATP-binding cassette (ABC) transport system from the pathogenic bacterium Haemophilus ducreyi. The structure of Hd-SatA in the native form and sialic acid-bound forms (with Neu5Ac and N-glycolylneuraminic acid (Neu5Gc)), determined to 2.2, 1.5, and 2.5 Å resolutions, respectively, revealed a ligand-binding site that is very different from those of the SiaPs of the TRAP transport system. A structural comparison along with thermodynamic studies suggested that similar affinities are achieved in the two classes of proteins through distinct mechanisms, one enthalpically driven and the other entropically driven. In summary, our structural and thermodynamic characterization of Hd-SatA reveals that it binds sialic acids with nanomolar affinity and that this binding is an entropically driven process. This information is important for future structure-based drug design against this pathogen and related bacteria. [ABSTRACT FROM AUTHOR]