Bbiochem Final Review Exam Ii

Front 1

in a polar aa, the R group contains....

Back 1

OH or an amide

Front 2

what class of molecules are neurotrans

Back 2

aa

Front 3

what are some examples of aa that are neurotrans

Back 3

GABA, glycine, glutamate, melatonin

Front 4

are hormone aa?

Back 4

yes

Front 5

carboxylation, hydroxylation, an dphophorylation are examples of how aa can be modified to form ____ _____ _____

Back 5

amino acid derivatives

Front 6

what do the R groups of ser, thre, and tyr all have in common

Back 6

an OH group that can be phosphorylated

Front 7

define the isoelectirc point

Back 7

the pH where the overall charge of the aa is zero

Front 8

the lower the pka the weaker or stronger the acid?

Back 8

stronger

Front 9

what aa have a basic structure at pH 7

Back 9

tyr
lys
arg

Front 10

is a peptide bond rigid and planar? if so why

Back 10

yes, partial double bond character of the peptide bond has resonance

Front 11

what does a schiff base look like

Back 11

imine C=N

Front 12

what is an example of a peptide that is a reducing agent

Back 12

glutathione where GSH goes to GSSG

Front 13

what are some functions of porteins

Back 13

catalysis
structure
movment
defense
regulation
transport
storage
stress response

Front 14

what is a holoprotein? apoprotein?

Back 14

prosthetic group
no prosthetic group

Front 15

what are some examples of conjugated proteins

Back 15

glycoproteins lipoporteins metalloproteins phosphoproteins hemoproteins

Front 16

why are gly and pro incompatible with an alpha helix

Back 16

they are too bulky

Front 17

what stabilizes beta pleated sheets

Back 17

H bonds

Front 18

what stabilizes tertiary structure

Back 18

hydorphobic interatction
electrostatic interactions
hydrogen bonding
covalent bonding
hydration

Front 19

what decreases heme's affinity for O2 and protects Fe2+ from irreversibly oxidizing to Fe3+

Back 19

heme protein

Front 20

does fetal hemoglobin have a higher or lower oxygen affinity

Back 20

higher affinity

Front 21

does myoglobin have a higher or lower oxygen affinity than hemoglobin

Back 21

higher

Front 22

what is the bohr effect

Back 22

dissociation of o2 from hemoglobin is enhanced at lower pH because H stabilizes the deoxy form of hemoglobin

Front 23

ligands that trigger allosteric transitions are called ____

Back 23

effectors or modulators

Front 24

enzymes tend to stabilize the _____ _____

Back 24

transition state

Front 25

dehydrogenase, oxidase, oxygenase, reductase, peroxidase, and hydroxlyase are all examples of

Back 25

oxidoreductases

Front 26

kinase is an example of

Back 26

transferase

Front 27

esterase phosphatase peptidase protease are examples of

Back 27

hydrolases

Front 28

what do lyases do

Back 28

remove a group and form a double bond or add a group to a double bond

Front 29

what are some exampels of lyases

Back 29

decarboxylase, hydratase, dehydratase, deaminase, synthase

Front 30

mutase racemase and epimerase are examples of

Back 30

isomerase

Front 31

what do ligases do

Back 31

bond formation that requires an energy source such as ATP

Front 32

synthases are ______ while synthetases are _______

Back 32

lyases
ligases

Front 33

carboxlyase is an example of a

Back 33

ligase

Front 34

in a first order reaction vx =

Back 34

k[S]

Front 35

if [s] doubles and rate double, the reaction is what order

Back 35

first

Front 36

in second order reactions vx =

Back 36

k[A][B]

Front 37

when would you see zero order kinetics

Back 37

saturation

Front 38

when would you see pseudo first order

Back 38

if one reactant is in excess such as water

Front 39

state the MM equation

Back 39

vo = (Vmax[S]) / [S] + Km

Front 40

what are the axes of the michaelis menton plot

Back 40

vo vs [S]

Front 41

what happens when [S] = Km

Back 41

then vmax/2 is vo

Front 42

kcat is the ____ number

Back 42

turnover

Front 43

kcat =

Back 43

vmax/total enzyme conc

Front 44

specificity constant =

Back 44

kcat/km

Front 45

what does specificity constant tell you

Back 45

an indication of subtrate binding effeiency

Front 46

the lower the km the lesser or greater the affinity for the substrate

Back 46

GREATER

Front 47

state the LW plot

Back 47

reciprocal of MM

1/vpo = km/vmax 1/[S] + 1/vmax

Front 48

what types of inhibition are reversible

Back 48

competitive
noncompetitive
uncompetitive

Front 49

competitive inhibitors bind to

Back 49

ative site of E

Front 50

noncompetitive effectors bind to

Back 50

both E and ES

Front 51

uncompetitive bind to

Back 51

ES not E

Front 52

definiton. the rate of flow of metabolites.

Back 52

metabolic flux

Front 53

what aa can you associate with covalent catlysis

Back 53

ser

Front 54

what are cofactors

Back 54

non protein components that add chemical functionality to enzymes and thus increaes the kinds of reactions that enzymes can catalyze

Front 55

_____ are precursors to coenzymes

Back 55

vitamins

Front 56

what are two methods of genetic control of enzymes

Back 56

enzyme induction
repression

Front 57

what are some examples of covalent modification of enzymes

Back 57

phosphorylation
zymogens