Students often struggle with visualizing protein structures when working with two-dimensional textbook and lecture materials, so introducing them to 3D visualization software developed by and for structural biologists offers them a unique opportunity to work with authentic data while furthering their spatial reasoning skills and understanding of molecular structure and function. This article presents an active learning virtual laboratory in which students use authentic structural biology data to investigate the effects of both hypothetical and real-world SARS-CoV-2 mutations on the virus’s ability to bind to human ACE2 receptors and infect a host, causing COVID-19. Through this activity, introductory-level college students or advanced high school students gain a better understanding of applied biology, such as how vaccines and treatments are designed, as well as strengthening their understanding of core disciplinary concepts, such as the relationship between protein structure and function and the central dogma of molecular biology. While there were challenges during the pilot phase of activity development due to COVID-19 restrictions, students in the pilot groups came away from the activity with deeper understanding of the relationship between proteins and amino acid sequences and a new appreciation for the ways researchers design treatments for and study viruses.
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Virtual Boot Camp: COVID ‐19 evolution and structural biology
COVID‐19‐related campus closures necessitated invention of an intensive online learning experience that introduced students to Structural Bioinformatics. The program engaged 33 students from 11 different institutions ranging from high school to graduate school. The objectives of the intensive, 1‐week Boot Camp focused on helping students build a foundation for studying the SARS‐CoV‐2 Main Protease (Nsp5) to understand how the protein evolved during the first 6 months of the COVID‐19 pandemic by exploring amino acid sequence and 3D atomic‐level structure using various structural bioinformatics tools. Participants analyzed how the protein changed as the virus spread around the world, comparing Nsp5 from the original viral isolate to 161 unique sequence/structure variants.
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- PAR ID:
- 10187212
- Date Published:
- Journal Name:
- Biochemistry and Molecular Biology Education
- ISSN:
- 1470-8175
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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