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Learning Objectives
Chapter 20 – Proteins
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What are the different roles that proteins play in the body?
What are the monomers in proteins?
What is the basic structure of an amino acid? What functional groups does it contain?
If I were to give you a page with the structures of the amino acids, you should be able to recognize and
name the different structures. You should also be able to look at the amino acids’ side chains and
determine if the amino acid is nonpolar, polar, acidic, or basic.
What does it mean if we say that some amino acids are “essential”?
Which amino acid is not chiral? (What does it mean if something is chiral?)
Which isomer is found in biological proteins?
What is a zwitterion?
Which form of amino acids exist at low pH? At neutral pH? At high pH?
You should be able to look at a structure and determine if the structure exists at high or low pH.
What does pKa tell you about the ionization of a functional group?
Which amino acids have ionizable side chains?
You should be able to use structures of amino acids and a pKa table to draw the step-wise ionization of
any of the 20 standard amino acids. You should then be able to use the step-wise ionization to
determine the charge an amino acid has at a particular pH.
What is electrophoresis? You should be able to determine the charge an amino acid has at a given pH
and predict the direction it will move during electrophoresis.
What is a peptide bond? What kind of a reaction forms a peptide bond? You should be able to draw
the resulting dipeptide that forms between two amino acids.
What does the protein “backbone” look like?
What are peptides? What are the conventions when drawing peptides (ie. Which amino acid goes on
the left? Which amino acid goes on the right?)
You should be able to name amino acids (based on their structures).
What is the difference between dipeptides, tripeptides, polypeptides, and proteins?
You should be able to determine the possible peptide sequences formed from individual amino acids
(see slide 27).
You should be able to look at a peptide structure and determine the order of the amino acids in the
structure, which acid is the N-terminal amino acid, and which amino acid is the C-terminal amino acid.
You need to know the four different levels of protein structure…what they are and what they are
caused by. You should be able to recognize a level of structure from a description of it.
What is the difference between alpha helices and beta pleated sheets? What interaction hold
secondary structure in place?
Which types of interactions hold three dimensional structure in place? Which amino acids are
involved in these interactions? You should be able to look at two amino acids and determine which
kind of interaction would occur between them (see slide 42).
What are the major differences between globular and fibrous proteins? You should know examples of
each of these types of proteins.
What is protein hydrolysis? What are the products of protein hydrolysis? What reaction conditions
are required for protein hydrolysis? You should be able to predict the products of the hydrolysis of a
particular protein.
What is denaturation? What does denaturation do to protein structures?
What are some common denaturants? How do they cause denaturation?
How do immunoglobulins recognize antigens?