AP Bio Protein Structure: Primary, Secondary, Tertiary, and Quaternary Structures

Primary structure

peptide bonds join amino acids in a specific sequence in a polypeptide

Secondary structure

The alpha helix and beta-pleated sheets form by hydrogen bonding between the atoms in the peptide bonds along the chain

Tertiary structure

A polypeptide folds into a compact, 3-D globular shape stabilized by interactions between R groups of amino acids to form a biologically active protein

Quaternary structure

Two or more protein subunits combine to form a biologically active protein

order and type of amino acids determine this...

primary structure

beta-pleated sheet is present in...

secondary structure

3D globular shape is present in...

tertiary structure (or quaternary structure)

disulfide bridges between R groups are present in...

tertiary structure (or quaternary structure)

covalent bonds are present in...

primary structure bonding all atoms together in a continuous chain

two hydroxyl groups may interact to form...

hydrogen bond

hydrogen bonds are present in...

secondary, tertiary (and quaternary) structures

alpha helix is present in...

secondary structure

Van Der Waals forces (London Dispersion) are present in...

tertiary (and quaternary) structures

acid/base interactions are present in...

tertiary (and quaternary) structures

two methyl groups interact to form...

Van Der Waals forces (London Dispersion)

Hydrogen Bond

interaction between hydrogen and a highly electronegative atom

peptide bonds are present in...

primary structure

Levels of protein structure affected by denaturation...

secondary, tertiary (and quaternary)

Bond or IM Force NOT affected by denaturation...

peptide bonds and all other covalent bonds in protein

Factors that may disrupt IM forces...

acid, base, heat, salt, and many others