This set of models is designed to be used to practice folding (and scoring) a protein structure in preparation for the Division C Protein Folding Event. A rubric and scoring guide are available on the CBM Science Olympiad Protein Folding website.
When proteins fold into their tertiary structures, there are often subdivisions within the protein, designated as domains, which are characterized by similar features or motifs. One such motif is the zinc finger, in which a specific domain of the protein is arranged into a "finger-like" structure where two β-sheet strands and one α-helix are positioned around a zinc ion. The zinc finger motif is commonly found in eukaryotic transcription factors, which are proteins that bind to specific sequences of DNA in order to regulate transcription.
One common class of zinc finger is the C2H2 class in which the zinc ion is coordinated (held in place) by two cysteine residues and two histidine residues. This Mini-Toober folding activity allows students to fold the polypeptide chain into the α-helix and β-sheets to produce the "finger-like" structure and to see the interaction of the sidechains of histidine and cysteine with the zinc ion. This activity can be used as a stand-alone activity, as an extension of the Amino Acid Starter Kit, or as preparation for the Science Olympiad Protein Modeling Event.
Models included in this Collection
- 4 Zinc Finger Folding Activity Sets
- 1 Mini-Toober
- 1 Mini-Toober Zinc Finger Folding Map
- 7 sidechains
- 7 metal clips
- 1 zinc atom
- Colored dots
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Milwaukee School of Engineering
1000 N. Market Street
Milwaukee, WI 53202-3113