7.1 Flashcards
what do all amino acids have in common?
they have a central carbon atom, and an amino ion, a carboxyl
what differs from monomer to monomer?
the side chain
what is primary structure?
the linear form/order of amino acids in a chain
what is secondary structure?
alpha helixes and beta pleated sheets, formed by hydrogen bonds between aminos and carboxyls
what is tertiary structure?
the final 3D shape of a single polymer, created by interactions between hydrophilic side chains, hydrophobic, cysteines, and acidic and basic.
what is quaternary structure?
more than one polymer chain bonded together
what happens during denaturation?
the secondary and tertiary structure are destroyed by disrupting hydrogen and ionic bonds. this can be caused by extreme temps, pH changes, and salinity changes
how do different side chains interact with each other in tertiary structures?
cysteines = disulfide bonds, acidic + basic = ionic bonds, hydrophilic = attracted towards outside of structure, hydrophobic = clump in center away from outside
what is the function of hormones?
they send messages through the bloodstream
what is the function of pumps, channels, and receptors?
why would the structure and function of a protein change when a hydrophobic amino acid is substituted for a hydrophilic one?
the change in the hydrophobic amino acid would change the way it bends, since it’s now folding towards the opposite way. since the structure of the protein changes, the polypeptides will fit together differently, causing the function to change.
How are the effects and results of protein denaturation different from the effects and results of a mutation?
a mutation changes the structure of the polymer and that can change the function. denaturation uncoils and unfolds the helixes and sheets. mutations just alter the structure of secondary and tertiary structures, while denaturation destroys them.
