Spring 2014 CHEM4165/5165

Pre-activity week 2

1) Review chapter 2 sections that discuss ionization, weak acids and weak bases. Work on HW#1 for
chapter 2 problems as needed to help you remember how to work buffer problems.
2) Read through chapter 3. Produce an outline for sections on amino acids and the section that introduces
the peptide bond.
3) Commit to memory the structures of the 20 amino acids, as well as their correctly spelled names, one
letter and three letter codes. Note which side chains are polar, non-polar, amphipathic, ionizable- which
amino acid side chains will carry a positive charge at neutral pH? Negative charge?
4) What is the zwitterion form of an amino acid? What does it mean to say that amino acids are
amphoteric? ampholyte? And what is the definition of the isoelectric point (pI)? How do you calculate
the pI for a polyampholyte given the pKa of each of the ionizing groups on that molecule? Draw an
arrow to the point on the titration curve for Histidine on figure 3-12b shown below that points to its pI.
5) Draw a titration curve for the amino acid lysine using the pKas of 2.2, 9.0 and 10.0 for each of the
ionizable groups of lysine. (Identify them: -carboxylate, -amino and side chain amino). Use the
model titration curve for histidine (figure 3-12b, shown below) and its labels, etc. as a model for your
drawing. Label the buffering regions and equivalence points. Draw the structures for the primary species
of lysine at all the buffering regions and equivalence points. Draw an arrow to the point on the curve
that corresponds to its pI.
6) Define the term buffering region and describe how you could locate the buffering region on a titration
curve.
7) Define the term equivalence point and describe how you could locate the equivalence point on a titration
curve.
8) Think about why the side chain amino group has a significantly different pKa than the -amino group.
(Hint: figure 3.11)