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Protein Folding (Stepping Stones-Full Activity)
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![]() | Overview and Learning ObjectivesIn this activity students discover how the properties of amino acids (charge and polarity) affect the shape of a peptide chain. They explore the complex interactions of amino acids with each other and with the surrounding water molecules or lipids. Sickle Cell Anemia is used as an example of a disease caused by a single amino acid substitution. Students will be able to:
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![]() | AssessmentUsing the knowledge you have gained in this activity, how would you explain the effect on a protein's activity of a point mutation in an enzyme? (Point mutation: substitution of one nucleotide in DNA that results in the substitution of one amino acid for another in the resulting protein molecule. This could possibly affect the charge on and the folded shape of the protein molecule.) |
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![]() | Classroom PracticeStudents need assistance in understanding that hydrophobicity is a lack of attraction to the polar water molecules and not a repulsion. The term hydrophobic itself is misleading, because hydrophobic amino acids don't actually repel water. Emphasize the idea that, as water molecules make hydrogen bonds with charged amino acids and with each other, non-polar molecules are pushed or herded away from water. To help students understand the concept of hydrophobicity, have students look at the model Hydrophobia: Activity #203 in this database. |
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![]() | Central ConceptsKey Concept: A peptide chain folds into a specific shape as a result of interactions of amino acids with each other and with the surrounding medium. One concept organization is available at: http://www.concord.org/~btinker/workbench_web/pdfs/Protein_Structure.pdf Additional Related ConceptsMolecular Biology
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![]() | Textbook References
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![]() | Benchmarks and StandardsAAAS
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![]() | Extensions and ConnectionsProtein folding is a logical precursor to such activities in the database as: Particular Proteins Insulin (Activity): http://molo.concord.org/database/activities/236.html Melittin (Demo) Protein: http://molo.concord.org/database/activities/87.html Hemoglobin Tour: http://molo.concord.org/database/activities/281.html Particular Functions Docking: Binding of Complementary Surfaces: http://molo.concord.org/database/activities/154.html Self-Assembly: http://molo.concord.org/database/activities/155.html |
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![]() | Activity CreditsCreated by CC Project: Molecular Logic and CC Project: Molecular Workbench using Molecular Workbench |
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![]() | Requirements
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Last Update: 08/05/2008
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Copyright © 2008, The Concord Consortium.
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These materials are based upon work supported
by the National Science Foundation under grant numbers
9980620, ESI-0242701 and EIA-0219345
Any opinions, findings, and conclusions or recommendations expressed in this
material are those of the author(s) and do not necessarily reflect
the views of the National Science Foundation.