Biochem final Flashcards

DNA
Terms Definitions
C5H12
Pentane
electron transfer
oxidation
H
His Histidine -CH2-C=CH-NH \ I N==CH
acitic acid
2 c
Hydrolysis of macromolecules
metabolism into acetyl COA
oxidation of acetyl
& oxidative phosphorylations
are all examples of what type of reaction?
Catabolic reactions
TTAGGG/CCCTAA are complements comprising what structure?
telomere
PO2 down
O affinity up
Chloramphenicol
antibiotic. prevents peptide bond formation
Uroporphyrin
coproporphyrin
Uroporphyrin: acetate & propionate side chains.
 
coproporphyrin: methyl & propionate side chains
Crigler-Najjar syndrome
UDP glucuronyl transferase deficiency
eukaryote
a unicellular or multicellular organism with cells having a membrane bounded nucleus, multiple chromosomes, and internal organelles
Endosomes are pre _________ compartments
lysosomal
V
Val Valine -CH - CH3 eSSENTIAL I CH3
parkinson's
lack of dopamine
solve: give L dopa/DOPA-decarboxylase inhib that doesnt enter brain.
 
What does PFK-1 synthesize?What does PFK-2 synthesize?
F-1,6-BPF-2,6-BP
Heme metabolism pathway: heme ->
biliverdinbilirubinconjugated bilirubin (in liver)urobilinogen (in intestine, by bacteria)stercobilin (feces) or urobilin (urine)
PPARgamma
promotes fat storage by increasing adipocyte differentiation and transcritpion of lipogenic factors
Cyanogen Bromide
cleaves peptide backbone, forms homoserine lactone
Gram negative bacteria have highly _____ outer membranes
Glycosolated
Duplication of double-stranded DNA is necessary for cell division. T/F?
true
isotopes
atoms of the same element with different numbers of neutrons
Practice Drawing use of muscle protein during fasting
-
ACE inhibitors
Angiotensin II receptor blockers
ACE inhib: vasoconstrictor "Pril"
Angiotensin II receptor blockers: Sartans
What is oxidation (general)
gives up electrons/reducing equivalents
Where do reducing equivalents from NADH enter the electron transport chain?
Complex 1
AngelMan's syndrome
Deletion of normally active Maternal allele. Mental retardation, seizusres, ataxia, inappropriate laughter ("happy puppet").
Pyruvate dehydrogenase complex
kinase phosphorylates serine which inactivates PDH**phosphorylated serine
What is biosynthesis of new glucose?
Gluconeogenesis (definition)
What special adaptation does theronyl-tRNA synthetase have for selectivity?
A zinc ion.
Transciption Initiation and Elongation
promotor recognizes
RNA polymerase forms
DNA unwinds
RNA polymerase initiates mRNA synthesis (almost always with purine)
RNA polymerase enlongates mRNA
sigma unit released
3 major kinds of lipids
glycerophospholipids, sphingolipids, cholesterol
where does gluconeogenesis occur?
cytosol of liver
cortex of kidney.
which clotting factors contain y-carboxyglu (gla domains)
2 7 9 10
Name the amino acid that donates the one-carbon group to FH4
Serine
Equilibrium
The point in a chemical reaction where the rate of the forward reaction is equal to the rate of the reverse reaction.
Duchenne's Muscular dystrophies
X-linked frame shift mutation -> deletion of dystrophin gene ->accelerated muscle breakdown. Weakness begins in plevic girdle muscles and progresses superiorly.Pseudohypertrophy of calf muscles due to fibrofatty replacement of msucle; cardiac myopathy. Use of Gower's maneuver, requiring assist of supper extremities to stand up, is characteristic. Onset before 5 years of age. Dystrophin gene is the longest known human gene -> incr rate of mutation. Dystrophin helps anchor muscle fibers, primarily in skeletal and cardiac muscle.
globular hemeproteins
protoporphyrin ring with an iron in middle
Type 1 Integral Proteins have the _______ end on the inside and the ________ end on the outside.
Carboxyl, Amino
func of DHEA?
weak androgen later converted to potent
post memopausal precursor for estrogen
inhibit G-6-P deH, reg. NAD+ coenzymes
Origin of Replication
specific point DNA double helix unwinds at
Direct apical sorting occurs in the trans golgi or the endosome
trans golgi
The two electrons at the beginning of ETS are being passed through what complex?
Complex 1
Name the B vitamin that must be obtained from the diet for the body’s synthesis of CoASH
Pantothenic Acid
Termination of translation
Release factors 1,2,3Stop codon in the A site.Ribosome stalls and RF-1 or 2 binds with RF3*GTP which bind the stop codon.This results in hydrolysis of peptidyl tRNA. Protein released.
what does the first step of fatty acid biosynthesis require?
ATP
what is the rate determine enzyme of ketogenesis?
HMG-CoA synthase
what are some important secondary active transportors in the body
symport=intestinal uptake of glucose/AAantiport=heart sodium/calcium
What are immunoglobulins?
Antibodies which are central to the humoral immune system of vertebrates.
Vitamin K is a _______
blood clotting co-factor

needed to activate clotting factors
Enter your front text here.
Enter your back text here.
tyrosine binding to it's receptor involves
(old exam)
tyrosine phospforylation of insuline receptor substrates
(old exam)
what happens to pyruvate?
oxidation (catabolism) to CO2 in TCA cycle
what happens to the F0 domain on the complex V as protons move from outside to inside
it rotates
What are the 3 ketone bodies
Acetone (we can't use it)Acetoacetatebeta-hydroxybutyrate
regulatory gene
a gene in front of the control site that produces a repressor
What biological effects do leukotrienes have?
Contraction of SM in pulmonary airway
-alternation in permeability of microvasculature, fluids leak into tissues
-D4 potent in muscle
retinal can be oxidized to give
retinoic acid, a hormonal signal
Palmitic Acid
 
1.  Use
1.  Added to low fat milk as a Vitamin A compound attached to retinol (alcohol form of Vit A) to stabilize the vitamin in milk
Go through steps how HIV retrovirus replicates itself
Viral RNA (with Reverse transcriptase)>>>Viral DNA (with integrase)>>>integrates into Host DNA "Provirus">>>makes viral mRNA>>>forms Viral poly protein (with HIV protease)>>>cuts into individual viral proteins
What does insulin do to muscles/adipose?(glucogen, TAG)
Decreases glycogen breakdown and TAG breakdown (lipolysis)
When in starvation what organs get the most amount of energy?
Brain, Heart and Kidney
what would you add to mixture of foreign already cut DNA and plasmid to join them.
ligase from T4 bacteriophage
What is the structure and class of myoglobin?
All alpha

Eight helices

Monomeric Globular unit, Soluble
Amino Acid Activation
The addition of an amino acid to the 3’ end of each tRNA
Requires:
amino acids
tRNAs
ATP, Mg2+
catalyzed by aminoacyl-tRNA synthetases
Give the alternative name for the ETC, and describe its location in a cell
Embedded in inner mitochondrial membraneAlternate name: Respiratory Chain
Which AA's don't have a three letter abbreviation that is the first three letters of its name? (4)
Isoleucine - ileTryptophan - trpAsparagine - asnGlutamine - gln
Excess Ile, Leu and Val in blood
Maple Syrup urine dzinability to degrade branched amino acids b/c of no alpha-ketoacid dehydrogenase
Common feature or structure of amino acid
alpha carbonH atomR side chain carboxyl group amino group
why fat storage energetically favorable over gylcogen?
get it faster and no extra waste, straight to kreb
Thylakoid is to _____ while Stroma is to _____
Thylakoid is to light reactions whileStroma is to dark
Integration 6g Citrate Lyase function
Citrate to OAA & acetyl CoA; takes an ATP
What is the energy released from steps in the ETC used for?
Pump protons from inner mitochondrial space to cytosol
biotin is a cofactor for _, and in one case, how is it regulated by phosphorylation?
propionic CoA carboxylase in gluconeogenesis and Acetyl CoA carboxylase that changes Acetyl CoA to Malonyl CoA in FA synthesis. ACC is inactivated when AMP dependent protein kinase phosphorylates it, so that FA synthesis doesnt occur when energy levels are low
plasmid is? example of gene found on plasmid?
circle DNA in bacteria
code for resistance
what is the first reaction of the TCA cycle?
combines acetyl CoA and oxaloacetate to form citrate
What is is a good indicator of how high a person's average blood glucose levels were over the previous several weeks
concentration of glycated hemoglobin A (hemoglobin A1c)
27 y.o. father diagnosed with huntingtons, important to?
do DNA sequencing to see if they will have it
What is the typical carboxyl group pKa range?What is the typical amine group pKA? For a double bond?
COO- is typically 2 to 4NH3+ is typically 9 to 10&C=NH2+ is ~ 12
If a tRNA is mischarged, will it still attach its incorrect A.A. to the corresponding codon?
Yes. tRNA's attached amino acid plays no part in codon selection.
how are sugars absorbed in the small intestine?
the PH of the SI is 6.0 to 7.o
when food enters, the low PH triggers secretion of secretin which triggers the pancreas to secrete bicarbonate to buffer. 
pancreatic amylase hydrolizes starch and glycogen. 
Thiol
SH
C1 unit?
?Bicarbonate
Y
Tyr Tyrosine -CH2-bENZENE-OH
eicosanoids
20C unsaturated
3 goups=prostaglandins, leukotrienes, and thromboxanes
What defines prolonged fasting?
Ketosis
Vitamin B6
Deficiency: convulsions, hyperirritability, peripheral neuropathy. Can be induced by INH or OCPs.
 
Function: converted to pyridoxal phosphate, a cofactor used in transmination (AST, ALT), decarboxylation and heme synthesis. Also a necessary cofactgor in the synthesis of delta-aminolevulinic acid which is increased in lead poisoning.
What are monomers
Amino Acids
Pyruvate Dehydrogenase mechanism
 
(Enzyme 1)
Runs the "set-up"
what activates plasmin?
tissue plasminogen activator
Biotin
Needed for carboxylation rxnsPyruvat carboxylase allows progression of TCAAcetyl-CoA carboxylation allows for oxidation of FAPropinoyl-CoA allows for the connection of FA oxydation to the TCA cycle
heparin
glucuronic acid and n-acetyl galactosamine in an alpha 1-4 bond
What enzyme catalyzes the rearrangement of disulfide bonds in the ER?
PDI
Cancer
 
1.  Most common protein mutation
1.  p53
Porphyrines
cyclic, binds metals,
4 pyrole rings linked by methenyl bridges
differ by side chains attached to the 4 pyrole rings
each pyrole can bind 2 side chains.  (IV different arrangements)  only type III asymmetric on ring D is physiologically important
Overall, where do high energy electrons from nutrients go and what do they form
oxygenwater
Acute intermittent porphyria
urobilinogen-1 synthase deficiency (heme synthesis)autosomal dominant but late onset and variable expressionpain in abdomenpolyneuropathypsych*pink urineprecipitated by drugs (*barbituates*, OCP, sulfa drugs)
Mechanism of hemochromatosis
Liver is underexpressing Hepcidin
mRNA
messenger RNA; produced in the nucleus by DNA to carry the genetic info to the ribosomes for the construction of a protein
Aminoacyl-AMP can also be called
Aminoacyl adenylate
________ is used to synthesize proteins.
RNA
change of G
reaction goes to teh right
Practice drawing figure 1.3 on page 4
-
How is Vit K recycled?
reduction (via reductase)
2 allosteric inhibitors of PFK-1
citrate and ATP
How many protons total are pumped out/NADH
10
Cri-du-chat syndrome
congenital microdeletion of short arm of chromosome 5findings: microcephaly, moderate to severe mental retardation, high-pitched crying/mewing, epicanthal folds, cardiac abnormalities
3 Sources of Pyruvate
1. lactate2. alanine3. glycolysis
Eukaryotic Transcription Initiation

What is the role of TFIIB?
Directs DNA's path through transcription complex.

Processivity factor: Stabilizes TFIID on DNA.
polyunsaturated fatty acid
double bonds create bends
less organized packing
potential for motion
Cells need to regulate supercoiling during _______________.
DNA replication
Rofecoxib (Vioxx)
Expensive NSAID that is COX-2 specific (also possibly increases risk of cardiovascular disease)
B-oxidation
The process by which fatty acids, in the form of Acyl-CoA molecules, are broken down in mitochondria and/or in peroxisomes to generate Acetyl-CoA
what kind of inhibition is penicillin
irreversible suicide inactivator
location of electron-transfer chain complexes
inner membrane of mitochondria
What is Delta E?
Difference in reduction potential between the oxidant and reductant
What does argininosuccinate lyase do?
cleaves argininosuccinate into fumarate and arginine
a.a. with basic side chains
these are proton acceptors 
histidine
lysine
arginine
Lysosomal Storage Disease
Mutation in the N-link glycosylation (glycoprotein tagging) of lysosomal enzyme leads to their deficiency
2 neuraminidase inhibitors?
Tamiflu
Relenza

Type A or B
Both are sialic acid analogs (bind to active site)
Prokaryotic vs. Eukaryotic DNA
Three vs. five main polymerases
Primase in prokaryotes, polymerases also act as exonucleases in prokaryotes and there is only one origin of replication, Okazaki fragments are much longer, no histones complexed with DNA
This family of GTP binding proteins is invovled with vesicle targetting.
Rab
Now have ATP reaction so we go where?
Dark Reactions
What two things work to completely activate muscle glycogen phosphorylase?
AMP & Phosphorylation
TRP operon
codes 5 protesin needed to make trp with is required for translation
how does the oxidative branch of pentose shunt begin (enzyme?)?
glucose-6-phosphate dehydrogenase converts glucose-6-phosphate to ribulose-5-phosphate
What is Vitamin B2?
Riboflavin, cofactor in oxidation and reduction. FAD and FMN are derived from riboFlavin. Def causes Cheilosis and corneal vascularization. Megenta colored tongue
what type of vitamins serve as hormone precursors
A and D
What is the protein class of calmodulin?
All-alpha

Two domains

Undergoes conformational change upon ligand binding.
"nuclear" receptors
48 in humans
- most receptors rside in cytosol
- upon ligand-binding, they dimerize -> sent into nucleus
- "slow-acting", mediate global cellular changes
- do not employ amplification cascades
what occurs in the cytosol?
glycolysis and pentose phosphate pathway
what is brittle diabetes?
high fluctuations in blood sugar verry high/ verry low
(bad insulin control)
Cholesterol 2gDescribe conversion of Mevalonate to The two interchangeable isoprene donors (3) (p. 641)Draw MevalonateDraw an isoprene
Mevalonate is phosphorylated and drops an H and adds two phosphates to become 5-pyrophosphate mevalonateIt is then again phosphorylated and becomes 3-P-5PP mevalonate Costs 3 ATP; one for each phosphorylationCarboxyl group CO2 and the 3-P is cut off to make Delta 3 Isopentenyl pyrophosphate ←→ dimethylallyl pyrophosphateIsoprene:CH2||C-CH3|CH||CH2
non-appressed regions of the thylakoid
Stromal lamellae
 
has PS1 and ATP synthase
 
has more NADP and ADP
What does carbamoyl phosphate synthetase I do? Where does this take place? What is the regulator of this enzyme?
makes carbamoyl phosphate from NH4+ and CO2 and 2 ATPs. The CO2 (as HCO3-) comes from mitochondrial respiration. Takes place in liver mitochondria. N-acetylglutamate positively regulates CPSI.
Bohr Effect
CO2 + H2O = H2CO3 = HCO3- + H
Name substrate and products of acetylcholinesterase?
acetylcholine --> acetate + choline
Ending of DNA replication
RNA primer is removed by DNA polymerase I as repliction fork moves away
2 Essential Fatty Acids and their form of omega
1.  Alpha-linolenic (Omega 3)
 
2.  Linoleic (Omega 6)
what is a bad side effect of using heparin?
HIT: heparin-induced thrombocytopeniaautoimmune response when antibodies are generated to a HMWH paltelet complex
Describe the rxn catalyzed by GSH reductaseAlso, what makes GSH unique as a peptide?
GSSG NADPH --glutathione reductase→ 2 GSH NADP+Ribosomes use a-carboxyl group to make peptides; GSH not made by a ribosome so the a-carboxyl group is not used
What do Rotenone, CN-, antimycin A, and CO do?
they are electron transport inhibitors
What is true of hydrogen bonds?
Hydrogen bonds form readily in aqueous solutionsIndividual hydrogen bonds are much weaker than covalent bonds.Hydrogen bonds account for the anomalously high boiling point of water.In liquid water, the average water molecule forms hydrogen bonds with three to four other water molecules.
why carnitine palmitoyltransferase I deficiency leads to hypoketosis?
build up of carnitine a ketone, durrr
How is the recombinant plasmid cloned?
The plasmid containing the inserted DNA is “transformed” into E.coli bacteria which replicates the plasmid

The inclusion of antibiotics in the growth environment means that only bacteria containing the plasmid will be able to replicate
How does branching enzyme work?
By transferring a link from 1-4 to 1-6
Significance of non reducing ends of glycogen.
Plentiful.Where action of building or breaking down of glycogen happens
what kind of cells are rich in SER?
liver hepatocytes and steroid hormones
21 hydroxylase deficiency leads to _ and _ not being made, causing _ to not occur resulting in too much _ which becomes too much _. _ and _ are symptoms
glucocorticoids are not made, so feedback inhibition of production of ACTH by the anterior pituitary does not occur, resulting in too much progesterone which becomes too much androgens (sex hormones). Gentalia development and growth problems are symptoms.
What are some of the effects that prostaglandins can have?
-stim. smooth muscle
-reg. steroid syn.
-inhibit gastric secretion
-inhibit hormone sensitive tissues
-inhibit platelet aggregation
-reg. nerve transmissions
-sensitize to pain
-mediate inflammatory response
Way electrons move around has to do with what?
Pigments- Beta carotone these are critical in electrons go from PS II to PS I
What is added to eukaryotic mRNA as they undergo extensive processing?
-CAP @5' END.N-7 methyl guanine attached to +1 by PDE bond.2 OH methylation3' Poly A tail.
What are the 3 classes of RNA polymerases?
 
What does each synthesize?
 
Which one is especially sensitive to a-amanitin?
RNA polymerase I - rRNAs
RNA polymerase II - mRNAs
RNA polymerase III - tRNAs (& other small RNAs)
 
RNA polymerase II is extremely sensitive to inhibition by a-amanitin
What are the three primary sources for carbon skeletons?
Lactate – produced during anerobic glycolysis
Amino Acids – derived from muscle protein
Glycerol- from triglycerides during lipolysis
Allowed pairings at the wobble position: 1st base of anticodon, 3rd base of codon
1. C
2. A
3. U
4. G
5. I
caugi
1st anticodon 3rd codon
C G
A U
U A G
G U C
I A C U
Cholesterol 5cSay how many carbons are in the structure of an unconjugated bile salt. Be able to recognize the chemical structure of an unconjugated bile salt. (3)
24 C’sC 25, 26, 27 missingC 24 becomes carboxyllic
what is the 3 structure of proteins
complete folding of aa chain in 3D space
How is mRNA moved along the ribosome?
With the help of Elongation Factor G, powered by the cleavage of GTP
What is the body's way of combating acidosis?
In the kidneys suck up glutamine when the body is in acidosis. The glutamine is then used to put ammonium ion in the urine, where you’re not only getting rid of ammonia (nitrogen) but also a proton.
Describe the action of a class II topoisomerase.
cuts both strands, pass some of the ermaining DNA helix between the cut strands , and reseals
A pregnant mother is adviced by her doctor to stay off of aspartame (Aspartate and Phenylalanine) (nutrisweet - found in diet coke), give me two reasons why?
She might have PKU or be a carrier and thus child might have it. And since the child is only screened at birth, she needs to have that diet restriction for atleast the first 8 wks - when the brian is developing.
suffix
tripsy
crushing
RDS glycolysis
PFK-1
normal platelet count?
150,000-450,000/mL
Primase
synthesizes RNA primer
PETER MITCHELL
1920-1992
 
-proposed the chemiosmotic hypothesis, in which electron transport chain acts as proton pumps, moving H+ from matrix to inter-membrane space.
-energy stored as electrochemical gradient
-ATP synthesis is driven by return flow of H+ via oxidative phosphorylation
Tay-Sacks disease
Progressive Neurodegeneration, developmental delay, cherry-red spot on macula, lysosomes with onion skin, no hepatosplenomegaly (vs Niemann-Pick)Hexosaminidase A defGM2 ganglioside accumulationAutosomal recessive
REGULATED STEPS OF CAC
A
what drugs stimulate insuline sensitivity?
good for DMI
avandia,actose
Draw cysteine's side chainDraw methionine's side chain
CH2-SHCH2CH2SCH3
LXR
Cholesterol sensor, governs transport, catabolism and elimination of cholesterol. Associated wth Tangier disease and sitosterolemia.
Peptidoglycans are structural polysaccharides made of _______ and _______ unbranched polymers
n-acetylglucosamine
n-acetyluramic acid
Ethane does not
have 2 consituational isomers
free fatty acids are transfered by
albunin
What is the maintained NAD+/NADH ratio
100/1
glucacotricoids (cortisol)
released when under stress
 
stop glyceroneogenesis in the adipose and help it in the liver by supressing/activating the PEPCK gene which makes PEP carboxykinase
 
the liver is stimulated to make TG but cannot store it and the adipose has been prevented from turning FA from blood into storeable TG so FA stay in the blood
 
this can cause insulin insensitivity
Velocardiofacial syndrome
22q11palate, facial, and cardiac defects
isoprenoids
backbone of 5C units
cholesterol is required for membrane synthesis, bile acid synth., and for prodxn of steroids
Ionophore-mediated ion transport sends ________ down an _________
ions, electrochemical gradient.
Multi-functional lipids, also known as terpenes
isoprenoids
Proteins pass through the translocon into the ER in a folded/unfolded state
Unfolded
Cristae Microcompartments special feature?
Evidently, cristae form microcompartments that restrict the diffusion of substrates and ions between the intercristal and intermembrane spaces. This has important functional implications because it would result in a locally greater pH gradient across cristal membranes than across inner membranes that are not part of cristae, thereby significantly influencing the rate of oxidative phosphorylation (Section 18-3).
Lysosomal Storage Disease
Tay-Sachs
what enzyme damaged?
what lipid buildup?
what symptoms?
lacks β-Hexosaminidase A
cant turn GM2 Ganglioside into GM3 Ganglioside
buildup of GM2 Ganglioside
Symptoms: retardation, muscular weakness, red macula, blindness
Integration 4iPhosphoenolpyruvate carboxykinase (PEPCK) function
fasting; turns OAA into PEP
Rubisco Form 2
In some photosynthetic bacteria.
Has 2 identical dimer subunits each with an active site.
Lack of ABC1
Tangier's Dz
 
inability for cells to excrete cholesterol
 
Low HDL and cholesterol collection in cells
antibodies are proteins produced by what cells?
B cells
Vmax is
K2[Et]rate of product formation times all enzyme concentration. 
Essential and non essential AA?
PVT TIM HALL
centromere
a specialized site in a chromosome, serving as the attachment point for the mitotic or meiotic spindle
Sequential interactions between these two agents facilitate nuclear transport
importin and FG-nucleophorin
A. phalloides
death cap mushroom. 90% of mushroom deaths. has alpha-amanitin- blocks RNA pol II- no mRNA synthesis
What is the function of CoA?
Carry acyl groups
Cholesterol 2aName tissues/organs that are the principal sites of cholesterol synthesis (2)
liver, gonads (ovaries, testacles)
Transporting Trioses to the Cytoplasm
Dependent on concentration gradients.
 
Starch can turn into maltose and glucose to be transported to the cytosol.
 
DHAP can also go from cholroplast to cytysol vit triose P antiportation.
 
 
purpose of NADPH
NADPH oxidase cofactor: PMN bacteria killingregenerates reduced glutathione: protects against ROS damage
# of hydrogen bonds each peptide bond forms
2
what enzyme can relax the negative supercoil of gyrase?
topoisomerase 1
What is the specific configuration of the amino acids involved in protein structure?
L-alpha-amino acid
Specific inhibitor of COX3
example?
COX3
acetaminophen
a pain reliever but bad for liver
In prokaryotes, the ___________ recognizes the __________ , which contains the ___________ of transcription
sigma () subunit
promoter
start point
in the net reaction, how many ATP's were used?
2
what type of receptor is the insuline receptor?
tyrosine kinase
function of reverse transcriptase?
turns viral RNA to viral DNA
Non-oxidative branch of pentose shunt reaction?What is it for?Reversible?EnzymesReaction?
Reversible (interconvert sugars containing 3-7 carbons)Rubulose 5p to ribose 5PNucleotide biosynthesisTransketoases-TPP as cofactorTransaldolases
What step is allostericaly regulated in the TCA cycle?Activated/Inhibited
isocitrate dehydrogenaseActivated by ADPInhibited by ATP, NADH
separates protein based on binding affinity for a specific ligand
affinity chromatography (more difficult; more information obtained)
pholphodiester bond
the phosphate link that joins the 3' hydroxyl grp in one nucleotide to the phosphate grp on the 5'-C atom in the next nucleotide
3 excitatory and 3 inhibitory neurotransmitters?
Excitatory: Acetylcholine, Dopamine, Histamine, Norepinephrine, epinephrine, glutamate.
Inhibitory: Glycine, Taurine, GABA,
Gene Therapy
The introduction of a gene into human somatic tissue to express a protein that is lacking due to mutation of that gene

Example:
Severe combined immune deficiency syndrome (SCIDS)

Patients have mutations in adenosine deaminase (ADA)
-affects T cell immune function
patients must live in a sterile “bubble”

The goal of gene therapy is to place a good copy of the ADA gene in the bone marrow of SCIDS patients
Familial breast cancer
mutation in BRCA1 or BRCA 2. double strand break repair
Two sources of propionyl CoAPropionyl CoA to Succinyl CoA requires...
Valine Isoleucine (made from AA's)Odd-chain FA'sPropionyl CoA + CO2 --Carboxylase--> Succinyl CoA
What happens to the SRP-ribosome complex in in the signal hypothesis?
Bound to the ER membrane.
Where are the elctron transfer chain complexes located?
Inner membrane of mitochondria
in a glycerophospholipids, what is usually attached to C(1) and C(2)?
C(1): saturated fatty acidC(2): unsaturated fatty acid
What are the 4 gluconeogenic enzymes that bypass the steps?
1. Pyruvate carboxylase
2. Phosphoenolpyruvate carboxykinase (PEP CK)
3. Fructose 1,6 bisphosphatase
4. Glucose 6-phosphatase
what tissues require ribose phosphate for high rate neucleotide synthesis?
bone marrow, skin, gastric mucosa
What is hyperchromicity?
UV absorbance at 260 nm increases with denaturation of DNA
what is the role of bile?
To break up fat into micelles
Cholesterol 3ePredict the effect of an increase in the concentration of AMP in a cell on the percentage of HMG-CoA reductase molecules that is phosphorylated
Increase in HMG-CoA reductase phosphorylation
If adipose can turn pyruvate into glycerol-3-phosphate then why cant it turn it into glucose?
because it has no phosphatases
# of amino acids per 360 degree turn
3.6 (collagen has 3)
What are the three glycolytic enzymes in gluconeogenesis?
1. Pyruvate kinase
2. PFK-1
3. Hexo/gluco kinase
1. Why is the citric acid cycle (c.a.c.) said to be amphibolic? What are its catabolic
functions? ...its anabolic functions? What are the other names for the citric acid cycle?
it degrades and synthesizes,
degrades-->oxdizes 2 carbons of acetyl CoA to CO2, gen reduced cofactors
syn-->starting materials can make glucose, aminos, fatties, heme
other names--> krebs, TCA cycle
step 1 of glycolysis
glucose + ATP -> glucose 6-phosphate + ADP
step by step mechanism of warfarin and coumeral
inhibits vitamin K reductase>>>keeps Vit KO in oxidized form>>>inactive>>>slows Vit KH2-dependent carboxylase>>>slows GLA formation>>>prothrombin won't bind to platelet membrane>>>prothrombin won't become activated
Describe your body’s synthesis of aspartate and asparagine from glucose (5)
glucose → pyruvate → (tca) → OAA
compare constant and variable regions of an immunoglobulin
constant regions form the structure of the antibody; IgG constant regions bind complement proteins and are sites for crossing of immunoglobulins across placental membranes
 
variable regions form the binding sites for antigens and haptens
Explain how each of the three buttressing bonds work to stabilize the 3-D structure.
1. Disulfide bonds: between two cysteine residues not necessarily close to each other
2. Salt Bridges: between acidic and basic chain groups or the N and C terminal amino acids
3. Hydrogen Bonds: Between side chain groups. (Between peptide bonds doesn't signify buttress bond).
What are the genetic elements of the lac operon
The regulator gene
the operator site
set of structural genes
How are fats and veg oils similar/different?
Veg oils are unsaturated and have double bond kinks
How and where are ketone bodies produced?Examples.
Made in the liver mitochondria from acetyl CoA that is produced there (buildup of it)Beta hydroxy butyrateAcetoacetateAcetone
reactions catalyzed by catalase
1) 2H2O2 --> 2H2O + O22) RH2 + H2O2 --> R + H2O
What is scurvy? Why does it occur?
a. weakness in the collagen structures due to no hydroxylation occuring in polypeptide chains leads to tooth loss, painful joints and easily damaged skin.
b. occurs due to lack of vitamin C which the body cannot make on its own but it crucial for hydroxylation.
Which is the only type of vesicle NOT to be associated with a ARF ATPase
COP II (associated with SAR1)
In which state is ATP made/NAD/NADH turned over? (Fed or Fasting)
Both. It doesn't matter b/c we always have to be ready for muscle contraction
What is the function of Ef:G?
Moves into the A site of the ribosome after peptidyl transfer
Hydrolyzes GTP to shove ribosome 1 codon down the mRNA.
Maltose is comprised of what two sugars joined by this type of link
Glucose with a alpha 1,4 linkage with glucose forms this disaccharide
heavy and light polypeptide chains within an immunoglobulin have an amino acid repeat containing how many amino acids?
110 AA (there are 2 in the light chain and 4 in the heavy chain)
What is the role of EF-TU GTP in the elongation phase of translation?
Binds aminoacyl-trna and brings to the A site. They bind to the acceptor stem of amino-acyl trnas.
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