A change here may result
in a nonfunctional protein
This is because the R goups may not
interact correctly changing the shape
of the protein and therefore the
shape of the active site.
Secondary
When the primary
structure folds to form
either a alpha helix or a
beta pleated sheet.
Tertiary
When the secondary structure folds again
due to the interaction of the R groups of the
amino acids. These can form Disulphide
bridges which are rare as only one amino
acid has sulphur in it. The attraction of
positive and negative ions. Hydrogen bonds
as well.
Quaternery
When one or
more polypeptide
chain is present
Small topic but requires
you to be able to apply this
to nearly everything so
learn it.