proteins Flashcards
elements found in all proteins
CHON
monomer of proteins
amino acids
common parts of amino acids
amine group, central carbon, hydrogen, carboxyl
parts of AA that differ
R group, hydrophobic or hydrophilic (polar or nonpolar), + or - charge
describe a carboxyl
COOH, O=C-OH
describe amine group
H2N, H-N-H
how does the shape of proteins react for hydrophobic/hydrophilic amino acids?
hydrophilic amino acids surround/fold around the hydrophobic amino acids
what occurs to form protein polymer
dehydration synthesis between carboxyl and amine group, forming peptide bonds between 2 amino acids
Defensive (internal defense) protein
identifying and killing disease causing organisms or particles, ex: antibodies- combats bacteria/viruses
Motor proteins (Movement/contractile)
contractile helps muscles move, ex: muscles
Enzymatic (Catalytic/digestive) proteins
speed up chem reactions, biological catalyst, ex: digestive enzymes- hydrolysis of polymers
Chemical messengers/peptide hormones (Regulation) proteins
chem messengers to coordinate activity & signal change, ex- insulin:helps regulate concentration of sugars in blood
structural proteins
provides physical support and protection, ex- collagen, elastin- animal connective tissue, keratin- hair, horn, feathers
transport proteins
carry around substances in body/membrane, ex: hemoglobin transports oxygen through blood
storage proteins
allows organisms to store AA as “food” for developing embryos, ex: egg whites- storage proteins, developing chick
how is one protein diff from another
diff sequence/structure of AA= diff functions
how do proteins get their unique 3D shape
the shape is determined by the # and order of AA
what does it mean for a protein to be denatured
unfolding of proteins, destroying the shape
causes of denaturing of proteins
change of temp or pH (acidity)
how does change of temp/pH make proteins denature
proteins are suited for specific environments, so with changes of pH or temp, it changes the shape of protein causing it to denature
name of protein polymers and describe their shape
polypeptide, unique 3D globular shape
describe primary structure
straight chain of AA (polypeptide), order & shape of AA determines func
describe secondary structure
alpha helix winds up and beta pleated sheets fold, held by hydrogen bonds
describe tertiary structure
helix or beta pleated sheets wraps around itself, making a 3D globular shape
describe quaternary structure
2 or more 3 degree proteins wrap around each other
