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Zinc Finger Folding Activity
Lending Library: Zinc Finger Folding Activity (ZA)
Teaching Points
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 in this Collection
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12 Zinc Finger Folding Activity sets
Documentation Included
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How do the models fit back in the suitcase?
Zinc Finger Folding Activity
MSOE Center for BioMolecular Modeling
Zinc Finger Folding Activity| 1
Model Details
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Each Zinc finger folding activity contains:
©
o 72 cm Mini-Toober with a red and a blue end cap
o Zinc finger folding map
o 7 foam amino acid sidechains:
 2 histidine
 2 cysteine
 1 phenylalanine
 1 arginine
 1 leucine
 Histidine and cysteine sidechains have two magnets each
©
o 7 metal Mini-Toober clips
o 1 orange or green zinc atom with magnets
o Sheet of colored dots
MSOE Center for BioMolecular Modeling
Zinc Finger Folding Activity| 2