Sickle Cell Disease
1. Identify and explain the primary, secondary, tertiary and quaternary structures of proteins and
the physiologic importance of protein folding.
a. Primary structure is characterized by the covalent bonding between the amino acids in
the linear structure (peptide bonds).
b. The alpha helices and beta sheets characterize secondary structure. These are defined
by the patterns of hydrogen bonds between the main chain peptide groups.
c. The folding of the alpha helices and beta pleated sheets characterize tertiary structure.
The constituents are folded into a compact globular structure. Hydrophobic interactions
drive the folding. Structure is made stable via salt bridges, hydrogen bonds.
i. Sequencing is important because it will determine the types of interactions seen
in the protein as it is folding.
d. Quaternary structure is stabilized by the non-covalent interactions and disulfide bonds
as the tertiary structure.
2. Describe factors that stabilize each order of protein structures.
a. Primary structure stabilized by covalent bonding interactions within the linear sequence
of amino acids.
b. Secondary structure stabilized by the hydrogen bonding intramolecularly, which aids in
the formation of the backbone to form a spiral shape
c. Tertiary structure is stabilized by salt bridges and hydrogen bonds and disulfide bridges.
