Transcript Quiz Next Tuesday (09/18) - Chemistry at Winthrop University

Quiz Next Tuesday (09/18)
Figure 4.18 Cation (a) and
anion (b) exchange resins
commonly used for
biochemical separations.
Figure 4.21
Chromatographic
fractionation of a synthetic
mixture of amino acids on
ion exchange columns using
Amberlite IR-120, a
sulfonated polystyrene resin
similar to Dowex-50. A
second column with different
buffer conditions is used to
resolve the basic amino
acids. (Adapted from Moore,
S., Spackman, D., and Stein,
W., 1958. Chromatography
of amino acids on sulfonated
polystyrene resins. Analytical
Chemistry 30:1185–1190.)
5.1 - What Is the Fundamental Structural
Pattern in Proteins?
Figure 5.3 The -COOH and -
NH3+ groups of two amino acids
can react with the resulting loss
of a water molecule to form a
covalent amide bond.
The Coplanar Nature of the Peptide Bond
Six atoms of the peptide group lie in a plane!
Figure 5.4
Anatomy of an
amino acid.
Except for proline
and its
derivatives, all of
the amino acids
commonly found
in proteins
possess this type
of structure.
5.2 – What Architectural Arrangements
Characterize Protein Structure?
• Proteins are classed according to shape and
and solubility
• Shape - globular or fibrous
• The four levels of protein structure
- Primary- Secondary - Tertiary –
- Quaternary -
Proteomics: Studying Protein
Structure and Function
-Proteins tend to be least soluble at their
isoelectric point
-Increasing ionic strength at first increases
the solubility of proteins (salting-in), then
decreases it (salting-out)
Gel Filtration
Chromatography
Affinity Chromatography
SDS-PAGE Electrophoresis