Connecting Protein Structure to Intermolecular Interactions: A Computer Modeling Laboratory

An understanding of protein folding relies on a solid foundation of a number of critical chemical concepts, such as molecular structure, intra-/intermolecular interactions, and relating structure to function. Recent reports show that students struggle on all levels to achieve these understandings an...

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Bibliographic Details
Published in:Journal of chemical education 2016-08, Vol.93 (8), p.1353-1363
Main Authors: Abualia, Mohammed, Schroeder, Lianne, Garcia, Megan, Daubenmire, Patrick L, Wink, Donald J, Clark, Ginevra A
Format: Article
Language:English
Subjects:
Biochemistry
Chemical Education Research
College Science
Computer Assisted Instruction
Computer based modeling
Folding
Inquiry
Laboratories
Laboratory equipment
Modelling
Molecular Structure
Organic chemistry
Protein folding
Proteins
Science education
Science Instruction
Science Laboratories
Scientific Concepts
Students
Undergraduate Students
Visualization
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Summary:An understanding of protein folding relies on a solid foundation of a number of critical chemical concepts, such as molecular structure, intra-/intermolecular interactions, and relating structure to function. Recent reports show that students struggle on all levels to achieve these understandings and use them in meaningful ways. Further, several reports show that the visualization techniques employed to help students understand protein structure often lead to confusion and propagate further misconceptions. Here, we report on a lab exercise using computer-based modeling to support student proficiency in using and making models and understanding H-bonding and the hydrophobic effect in the context of protein folding. We analyzed student drawings and explanations of protein structure and found significant improvements from pre- to postlab, indicating that students improved their understanding of protein folding. Further, we report on how we systematically refined our laboratory materials based on student work.
ISSN:0021-9584
1938-1328
DOI:10.1021/acs.jchemed.5b00910