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Draw the generalized amino acid structure,
identifying the amino group, the carboxyl
group, the radical group, and the alpha
carbon.
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Define what is meant by “essential amino
acid.”
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Explain how the characteristics of R groups
(polar, non-polar, and ionic) affect their
behavior in protein folding.
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Describe polypeptide chain formation in
terms of the formation of peptide bonds and
condensation reactions.
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Determine the number of peptide bonds given
the number of amino acids in a polypeptide.
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Describe the primary structure of a protein,
including the type of bonding involved.
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Describe the secondary structure of a
protein, including the type of bonding
involved.
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Describe the tertiary structure of a
protein, including the types of bonding
involved.
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Describe the quaternary structure of a
protein.
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Explain the role of chaperones in protein
folding.
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Contrast the structure of globular proteins
with the structure of fibrous proteins.
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Define denaturation and list conditions that
can cause it to happen.
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Define proteomics.
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Contrast the generalized function of
globular proteins with generalized function
of fibrous proteins.
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List and describe examples of fibrous
proteins used in structure and support.
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List and describe examples of fibrous
proteins used for movement and contraction.
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List and describe examples of globular
proteins used for storage.
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List and describe examples of globular
proteins used for transport.
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List and describe examples of globular
proteins used as hormones.
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List and describe examples of globular
proteins used as receptors.
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List and describe examples of globular
proteins used in defense against disease.
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List and describe examples of globular
proteins used as enzymes.
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Explain the role of mis-folded proteins in
disease (specifically Alzheimer’s).