Levels of Protein Structure

Primary structure: sequence of amino acids that forms the protein. All proteins have a
special sequence of amino acids, this sequence is derived from the cell's DNA.
(e.g. insulin )



Secondary structure: formed when the polypeptide coils or folds. This coiling and folding
forms a Alpha helix or Beta pleated sheet which are the basic form.
(e.g. actin, myosin)
Hydrogen bonds hold the coils in place. The bonds are weak, but numerous
throughout the molecule which provides stability.
Secondary structure refers to coiling and pleating of parts of the polypeptide
molecule



Tertiary structure: refers to the overall 3D structure of the final polypeptide/protein mole.
The tertiary structure forms when the secondary structure folds in on itself
(e.g. enzymes such as lipase, sucrase)
The 3D structure forms when the coils and pleats fold again. The 3D is held by
various bonds and interactions
The tertiary structure (the 3D shape is vital to the function) - e.g. enzymes and
their active site. The active site must be complementary to the substrate
molecule.

Bonds that stabilise tertiary structure are:
Disulfide bonds: Cysteine (an AA) contains sulphur. When 2 cysteines come
close together a covalent bond forms.
Ionic bonds: If the 'R' groups are charged, then oppositely charged AAs can form
ionic bonds.
Hydrogen bonds: When slightly - charged groups come into close proximity of +
charged groups, hydrogen bonds form.

Hydrophobic and Hydrophilic interactions also maintain stability in the tertiary
structure: these interactions occur in a water-based environment. Hydrophilic
AAs on the outside and hydrophobic AAs on the inside of globular proteins.




Quaternary Structure: a complex structure formed by the interaction of 2 or
more polypeptide chains. The quaternary structure is how 2 or more polypeptides form a
single protein molecule
(e g. haemoglobin)