Module 4- proteins- AP bio

Monomers of proteins

Amino acids

Protein’s shape and function

exact order or amino acids in a protein

amount of amino acids

20

Basic amino acids

positively charged r-groups

acidic amino acids

negatively charged r-groups

location of molecules with hydrophobic r groups in a protein

clustered together and buried in the interior of folded proteins

location of hydrophilic amino acids with hydrophilic r groups.

The outer surface of a folded protein

r groups that form ionic bonds with each other

charged r groups, positive or negative

covalent bond formed when two cysteines are close together

S-S disulfide bond.

What all amino acids share

carboxyl group, an amino group, hydrogen atom.

peptide bond

bond where a carboxyl group of one amino acids covalently bonds to an amino group of another acid, dehydration synthesis

polypeptide

a long polymer of amino acids

peptide

a short polymer of amino acids

primary structure of a protein

the order of amino acids in a protein

secondary structure of a protein

interactions between stretches of amino acids in a protein, alpha helixes and beta sheets

alpha helixes and beta sheets are slightly bonded to each other ( not covalently or ionically) via:

hydrogen bonds

tertiary structure

the overall 3d shape of a single polypeptide chain

denatured protein

when a protein is unfolded separates tertiary structure, deactivates protein

quaternary structure

arrangement and assembly of 2+ separate protein chains into a singular complex.