Biochemistry Flashcards
AA structure includes
basic amino group, acidic carbonyl group, R group, H atom
L-AA are used to
synthesize proteins
AA under low pH conditions =
protonated
AA under high pH conditions
deprotonated
_ AAs can destabilize or break down alpha helical 2 structures
glycine and proline
proline does NOT contain an
aromatic ring
_ AAs are the target of phosphorylation b/c they contain a hydroxyl functional group
serine, threonine, and tyrosine
_ AAs can form salt bridges
basic & acidic
_ can be used to break disulfide bonds in a western blot
BME
peptide bond
dehydration reaction in which the amino group of 1 AA acts as a nucleophile and attacks the carboxyl group of another AA, releasing a water molecule
amino and carboxyl functional group form a
amide group
formation of a peptide bond is a _ reaction
endergonic (E from ATP)
_ bonds stabilize secondary structure
H
_ structure forms optimal conformation of a protein
tertiary
what are the different forces stabilizing peptide bonds?
H bonds, ionic bonding/salt bridges, D-D interactions, LDF, and disulfide linkages
proteins fold into a state that _ the entropy of the system
maximizes, but minimizes their own energy
causes of protein denaturation
temperature, salinity, pH
solvation layer
water molecules that surround a protein
isoelectric focusing
each protein migrates until its reaches its pI
pH < pI =
+ charged
pH > pI =
- charged
native PAGE
separates proteins in their native tertiary state based on size and charge
SDS PAGE
separates proteins only based on their molecular mass NOT charge
western blot
proteins are visualized on a gel to see if a particular protein is present
formation of ES complex _ activation energy
lowers
oxidoreductase
transfer of electrons which result in change in oxidation state
transferase
transfer of a functional group from 1 molecular to another
hydrolase
breakdown of a covalent bond using water
lyase
breakdown of a covalent bond without water or electron transfer (oxidation)
isomerase
rearrangement of bonds within a molecule
ligase
formation of a covalent bond between 2 large molecules
enzyme approximation
enzyme catalyzes the reaction by bringing reactants in close proximity
covalent catalysis
enzyme catalyzes the reaction by forming a temporary covalent bond with the reactant
acid-base catalysis
enzyme catalyzes the reaction by acting as a n acid/base
metal ion catalysis
enzyme catalyses the reaction by assisting in electrophilic or nucleophilic interactions/binds to substrate
cofactors
inorganic ions (like iron or magnesium) that aids in activity
coenzymes
organic helpers and vitamins that aid in activity
2 ways to affect enzyme kinetics
increasing substrate concentration, increasing enzyme concentration
increasing substrate concentration beyond vmax effect:
none since the enzyme’s AS is already saturated
competitive inhibition
bind to AS, Km increased Vmax no change
non-competitive inhibition
bind to enzyme at allosteric site, no change in Km, decrease in Vmax`