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