Bio Biochem Strategies Flashcards
insulin will do whatever it can to
reduce sugar
pyruvate and amino acids relationship
aa are broken to make pyruvate
is NAD or NADPH needed to make a fatty acid
NADPH
Acetyl-CoA and NADPH make them with enzymes
what end is hydroxyl
3’
differentiate Arrhenius, Bronsted-Lowry, and Lewis bases
Ar– has OH
BL– can gran H+
Lewis– e- rich
base always becomes more positive after the acid does its thing
upregulation
make more of something
what powers ATP synthase
energy, as ATP, NADH, and FADH2
what is a metabolite
an intermediate
what is moving and what is not changing in decouplinng
H is moving, ATP is not changing
what does glucagon do to glycogen
turns it into glucose
where do you never debranch from
from the reducing ends
fast Vm means what for specificity
high specificit
what direction is spontaneous
unidirectional
will energy of enzyme transition state be high or low ?
higher
catalytic turnover formula
Vmax/Km = Kcat
1,6 vs 1,4 glycosidic bonds
1,6– branched
1,4– linear
GLUT-2 vs GLUT-4
2– liver (storage), B-cells (sensor), up Km
4– adipose tissue and muscle, stimulated by insulin + skeletal muscle; down Km
what peptide hormone upregulates glycogen synthesis
insulin
what peptide hormone inhibits gluconeogenesis
insulin
what peptide hormone promotes lipid storage
insulin
what peptide hormone inhibits proteolysis
insulin
glycogen
stored form of glucose that is broken down into glucose when the body is hungry
relationship between citrate and glycolysis
regulator of phosphofructokinase-1, which catalyzes the rate limiting step of glycolysis
Can I Keep Selling Sex For Money Officer
citrate
isocitrate
a-ketoglutarate
succinyl CoA
succinate
fumarate
malate
oxaloacetate
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Glucose
Glucose 6-Phosphate
Fructose 6-Phosphate
Fructose 1,6-bisphosphate
Glyceraldehyde 3-phosphate
1,3-Bisphosphoglyerate
3-Phosphoglycerate
2-Phosphoglycerate
PEP
Pyruvate
Glycolysis formula
Glucose + 2NAD + 2ADP + 2P -> 2Pyruvate + 2ATP + 2NADH + 2H
2 main enzymes to make glycogen
glycogen synthase and branching enzyme
what peptide hormone inhibits fructose 1,6-bisphosphatase
insulin
products of the PPP
NADPH and sugars (ribose-5-phosphate)
when is AMP-activated protein kinase
when energy in body is low
how does the reduction potential through the ETC progress
gets more positive
steric constraints in aa is related to:
size, bigger size = more constraints
This can overcome the structure of proline issue if its much bigger
which amino acids can act as nucleophiles
if they have a thiol (-SH) or hydroxyl (-OH) group.
which aa has a thiol group
cysteine
what are the types of electrostatic interactions
ionic bonding and hydrogen bonding
what type of interaction is salt bridge
electrostatic
how is peptide bond rotation?
restricted
which are the alkyl side chains? and which is not branched?
AVLIP
P
bicarbonate buffer equation
CO2 + H2O <-> H2CO3 <-> H + HCO3
does blood pH depend on O2 or CO2 ?
CO2
Gram (-) color and thickness
pink, and thin
women love pink, they’re always negative, and thin skinned.
Gram (+) color and thickness
purple and thick
Barney because he’s a thicc (thick wall) purple (color seen) dinosaur and was positive all the time.
how does increased CO2 affect blood pH
reacts with water to make H2CO3, which dissociates to form H+ and HCO3-
thus, increasing H+ concentration which lowers pH
response to low blood pH
increased breathing to exhale more CO2
hemodialysis
net fluid flow into the capillaries
endothelial cells
the cells in the simple epithelium
does the endothelium contract with the smooth muscle in vessels?
no
what gas particle sizes does heme have more affinity to
small.
why CO binds better than CO2
why when acidic, which makes H+ bind, O2 doesnt bind as well
ductus arteriosus and venosus =
fetal breathing
do veins or arteries have valves ? why ?
veins do, cause they prevent backflow of blood carried to the heart
what curve shape is cooperative binding, subunits, and example
sigmoidal, multiple, hemoglobin
an enzyme would be hyperbolic
albumin involved in what ?
osmoregulation, pH buffer, transport materials in blood
what cells is myoglobin in ? and how many subunits does it have ?
skeletal; 1
erythropoietin
a peptide hormone released by the kidney to tell the bone marrow to make more blood cells when there is low O2
do veins or arteries have valves
veins
what do ADH and Aldosterone increase the reabsorption of ?
water; salt
which type of vessel has the largest area, and how does this impact velocity
capillaries, blood moves slow
where and how many Na+ and K+ ions are transferred by Na+/K+ ATPase
3 Na+ out, 2 K+ in
(3 symbols in Na+ and o u t )
do reflexes require the brain ?
no, they are unconscious
FLAT PEG
what is released by the anterior pituitary:
- FSH
- LH
- ACTH
- TSH
- prolactin
- GH
bone resorption means
break down of bones, done by PTH
can self-antigens be in unhealthy cells
no
what do cytotoxic T cells need to work ?
signals from other immune cells
microvilli =
increased surface area
hepatic
liver
what vitamins are water soluble
B and C, all others are fat-soluble (stay in lipids)
path of proteins on ribosomes in the RER to the membrane
RER -> golgi -> vesicles -> membrane
how do filaments help address force
they (keratins for ex) help resist mechanical force
where do non-disjunction errors occur– P M A T
anaphase
think natural selection only before what age
reproductive age,
cause if the person shows problems after reproducing, they’re adding to the population. but if its before reproducing, they cant pass it on
endoderm
breathe and digest
(BED)
mesoderm
musculoskeletal
circulatory
reproductive
urinary
(MaCURh)
ectoderm
nervous
integumentary
nose, mouth, anus
ecto is a weird word like bugs
histone charge
positive / alkaline
positive control mechanism
the presence of the recipient will increase binding
what do operons do
one promoter and operator control many genes at the same time
does RAAS lead to vasoconstriction or dialation
vasoconstriction
how does the hypothalamus respond to low thyroid levels or high temperature
secretes TRH
Competitive plot
two light sabers crossing, cause they competitive
Uncompetitive plot
same line shifts Up
(u for up and uncompetitive)
Noncompetitive plot
Non-km-petitive
(Km does not move, so the x-axis is the same)
competitive binding site
COMPETES with the substrate for the active site,
so, binds at the active site
Uncompetitive binding site
ONLY binds to the ES- complex
(UNO)competitive
Non-competitive binding site
binds to active site and ES-compex equally
(no preference)
Competitive effects on Km
Km-petitive, so, Km increases
(the only one where Km increases)
Uncompetitive effects on Km
UN (kmpetitive)
so, Km decreases
Noncompetitive effects on Km
NON
Km does NOT move
pKa of carboxyl group vs amino group
2 vs 9
zwitterion when
it is about 7 or in between the pKas of the carboxyl and amino group
what is protenated and deprotenated in the zwitterionic form
COO- (carboxyl deprotenated)
NH3+ (amino group protenated)
under what conditions does the liver produce ketone bodies ?
glucose-poor (fasting) conditions
how many NAD+ per pyruvate
2
michael-menton equation
Vo = Vmax ( S / Km+S )
do catalysts affect Gibbs free energy ? Why ?
No, because gibbs is only dependent on the identities of the products and reactants
what type of bonding occurs in phosphorylation and glycolysation ?
covalent bonding between amino acid residues and other chemical groups
action potentials only occur in
channels and pumps
how do antagonists work ?
they bind instead of the agonist, and go inside to stop the reaction that the agonist would have had
Is GC or TA content more stable ? and why ?
GC, because they are triple bonded
spleen functions
immune and blood
when are disulfide bonds distrupted in SDS-PAGE
reducing conditions
Net Yield of Glycolysis
2ATP 2NADH 2pyruvate
(rule of 2s)
rate-limiting enzyme in glycolysis
phosphofructokinase-1
fructose-6p -> fructose 1,6 bisphosphate
ATP -> ADP
3 irreversible steps of glycolysis
- hexokinase / glucokinase
- phosphofructokinase
- pyruvate kinase
where does glcolysis occur
cytosol
rate limiting enzyme of krebs
isocitrate dehydrogenase
isocitrate -> a-ketoglutarate
NAD+ -> NADH
CO2
rate limiting enzyme of gluconeogenesis
fructose 1,6 bisphosphatase
rate limiting enzyme of glycogenesis
glycogen synthase
rate limiting enzyme of glycogenolysis
glycogen phosphorylase
rate limiting enzyme of PPP
glucose 6P-dehydrogenase
NADP+ -> NADPH
top and bottom of SDS Page
top– larger
bottom– smaller
top and bottom of Native Page
top– larger and (-)
bottom– smaller and (+)
top of thin layer (normal)
top– non-polar
what elutes first in column chromatography
the stuff you dont want
what elutes first in size exclusion chromatography
most volatile (low BP, less polar) elute first
what amino acids are glucogenic
all but lysine and leucine
E = hc(lambda)f
E = (hc) / lambda = h(lambda) = c(lambda)
FLAT PEG
follicle stimulating hormone (FSH)
luteinizing hormone (LH)
adrenocorticotropic hormone (ACTH)
thyroid-stimulating hormone (TSH)
prolactin
endorphins
growth hormone (GH).
How many H+ per ATP NADH and FADH2
4, 10, 6
Vm and specificity relationship
direct
catalytic efficiency
Kcat / Km
catalytic turnover
Kcat = Vmax / Km
how to dimerize
disulfide bond addition
Arrhenius base
has OH
Bronsted-Lowry base
can grab H+
Lewis base
has lone pairs and is electron rich
upregulate
downregulate
make more of something
make less of something
what does acid in water do to reach an equilibrium
will give a (+) at a pH of 7
do arteries have more O2 or CO2
more O2, except for the pulmonary
arteries carry blood away from the heart to body
more protons per electrons makes it tighter or looser ?
tighter
so, a positive metal will be smaller than a neutral one
e- is freedom, p+ is control
enantiomer
flipped
diastereomer
multiple stereocenters, with some flipped
are monosaccharies diatereomers?
yes– glucose, lactose, mannose
parts of a flagellum
basal body, hook , filament
where and in what conditions does glycolysis happen
bacteria, eukaryotes, aerobic, or anaerobic
where do Krebs and ETC happen and in what O2 conditions
mitochondria, and need O2