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Students often self-identify as visual learners and prefer to engage with a topic in an active, hands-on way. Indeed, much research has shown that students who actively engage with the material and are engrossed in the topics retain concepts better

Students often self-identify as visual learners and prefer to engage with a topic in an active, hands-on way. Indeed, much research has shown that students who actively engage with the material and are engrossed in the topics retain concepts better than students who are passive receivers of information. However, much of learning life science concepts is still driven by books and static pictures. One concept students have a hard time grasping is how a linear chain of amino acids folds to becomes a 3D protein structure. Adding three dimensional activities to the topic of protein structure and function should allow for a deeper understanding of the primary, secondary, tertiary, and quaternary structure of proteins and how proteins function in a cell. Here, I review protein folding activities and describe using Apps and 3D visualization to enhance student understanding of protein structure.

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    Title
    • From Pipe Cleaners and Pony Beads to Apps and 3D Glasses: Teaching Protein Structure
    Date Created
    2014-12
    Resource Type
  • Text
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    Identifier
    • Digital object identifier: 10.1128/jmbe.v15i2.714
    • Identifier Type
      International standard serial number
      Identifier Value
      1935-7877
    • Identifier Type
      International standard serial number
      Identifier Value
      1935-7885
    Note
    • The final version of this article, as published in Journal of Microbiology & Biology Education, can be viewed online at: http://www.asmscience.org/content/journal/jmbe/10.1128/jmbe.v15i2.714

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    This is a suggested citation. Consult the appropriate style guide for specific citation guidelines.

    Marshall, P. A. (2014). From Pipe Cleaners and Pony Beads to Apps and 3D Glasses: Teaching Protein Structure. Journal of Microbiology & Biology Education, 15(2), 304-306. doi:10.1128/jmbe.v15i2.714

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