proteins, enzymes and ATP Flashcards
(21 cards)
what three groups make up an amino acid
amino group
r group
carboxylic acid group
what is the amino group
H-N-H
what is the carboxylic acid group
OH-C–O
how many naturally occuring amino acids exist
20
what type of reaction occurs when two amino acids form a dipeptide
condensation reaction
what are the four levels of structure in protiens
- primary
- secondary
- tertiary
- quaternary-
what are the the bonds in proteins
- hydrogen bonds
- hydrophillic / phobic interactions
- ionic bonds
- disulfide bonds
what secondary structures of protein are there
- alpha helix
- beta pleated sheets
What is the difference between tertiary and quaternary structures
quaternary has two or more chains of polypeptides interlinked with eachother
what are polar molecules
partial negatives and partial positives charge on the two atoms
describe how peptide bond is formed between two amino acids to form a dipeptide
a condensation reaction occurs between the amino group and the carboxylic acid group
the secondary structure of a polypeptide is produced by bonds between amino acids - describe how
hydrogen bonds forming forming beta - sheets and alpha - helix
what type of proteins are enzymes
globular proteins
what do enzymes do
speed up rate of reaction
lowers activation energy without being used up
what is the lock and key model
substrate fit exactly into the shape of the enzyme
what is the induced fit model
enzyme changes the shape of its active site according to the shape of the substrate
describe how the monomers join to form the primary structure of a protein
monomers join together in a condensation reaction to form a peptide bond. Process repeats and creates a sequence of amino acids
what is the effect of PH on enzyme reaction
acid has H+ ions and alkali has OH- ions
interact with protein structure and alters ionic and hydrogen bonds
tertiary structure changes therefore active site changes and substrate no longer fits
what is a competitive inhibitors
binds to enzyme active site
similar structure to substrate
slows production
mostly reversible
what is a non competitive inhibitor
binds to the allosteric site on enzyme
alters the shape of the active site so substrate can no longer fit
slows production
what is the use of ATP
when broken down releases a quick large amount of energy
transfers within cells
