proteins Flashcards
(25 cards)
proteins in a low pH turn into
cations with a positive charge
NH3 +
protiens in a high pH turn into
anions with a negative charge
COO-
proteins in a neutral pH turn into
zwitterions both a positive and negative bit
aliphatic amino acids R groups
(phucking boring)
hydrocarbon chains
glycine
aromatic amino acids R groups
aromatic rings
phenylalanine
sulfur containing amino acids R groups
smelly cysteine and methionine
basic amino acids R groups
(Lucy ‘ine is basic)
have another NH2
lysine
acidic amino acids R groups
(aspartates tastes sour)
another COO-
aspartate
polar amino acids R groups
another OH
Snowy serine
miscellaneous amino acids R groups
proline
pro at being different
5 forces that hold tertiary structure together
van der walls
ionic
hydrogen
disulphide
hydrophobic
3 conjugated proteins
(basically they have quaternary structure)
glycoproteins
lipoproteins
metalloprotein - iron in heamoglobin
what do lipoproteins do
transport hydrophobic molecules- e.g cholesterol
whats a cofactor
a non protein component needed for a reaction
magnesium
whats a coenzyme
a heat stable substance that can aid in reactions
FAD from riboflavin
whats an isoenzyme
enzymes that catalyze the same reaction but vary in structure and other biochemical properties
how do enzymes lower the activation energy
entropy reduction
desolvation- takes it out of solution
induced fit
what does Km mean
how specific an enzyme is for the substrate
Km values
low= good fit
high= poor fit- takes longer
whats Vmax
how fast a reaction goes when enzyme is saturated
competitive inhibitor
sits in active site
can be overcome
non competitive inhibitor
sits away from active site
permanent
Vmax and Km for competitive inhibitor
vmax unchanged
Km increases
Vmax and Km for non competitive inhibitor
Vmax decreases
Km unchanged
