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Use of a protein scavenger hunt as a review activity in an upper‐division biochemistry course
Author(s) -
Mann Francis M
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.751.6
Subject(s) - protein secondary structure , protein quaternary structure , protein tertiary structure , folding (dsp implementation) , peptide , amino acid , code (set theory) , mathematics education , psychology , chemistry , computer science , biochemistry , engineering , programming language , set (abstract data type) , protein subunit , electrical engineering , gene
The composition, structure, and folding of proteins is a common topic in upper‐division biochemistry courses. In this 65 student course, student learning objectives include recognizing and reciting amino acids by structure and abbreviation, predicting structural changes due to pH, formation of secondary structures, and folding peptides into tertiary and quaternary structures. In order to review and self‐assess learning prior to an exam, students worked in groups to analyze clues in a four‐tiered scavenger hunt. Tier one consisted of locational clues written in single letter amino acid code leading to commonly recognizable campus locations. Tier two consisted of calculation of net charge on a small peptide in order to unlock a clue directing them to the next location. Tier three asked the students to decode a locational code by folding aligning a primary sequence on a secondary structure. The final tier asked students to fold peptide sequences into a quaternary structure with a specific motif and return to their instructor with the completed model. Common errors in deciphering of clues routed students back to their instructor early for group tutoring and concept correction prior to continuing on the hunt. Post‐activity student evaluation indicated students agreed that this activity helped them practice their amino acid recognition (73.4%), identify holes in their knowledge (81.4%), and the activity was better than attending a review lecture (82.2%). Overall, this activity serves as an engaging method for reviewing topics associated with protein structure.