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BCHM |\ 270 |\Midterm |\EXAM |\WITH |\
CORRECT |\ANSWERS
TCA |\Cycle |\Step |\ 1 |- |\CORRECT |\ANSWERS |\✔✔citrate |\synthase oxaloacetate |+ |\Acetyl |= |\Citrate |+ |\CoA TCA |\Cycle |\Step |\ 3 |- |\CORRECT |\ANSWERS |\✔✔isocitrate |
dehydrogenase isocitrate |--> |\alpha-ketoglutarate |+ |*NADH* |+ |\CO TCA |\Cycle |\Step |\ 4 |- |\CORRECT |\ANSWERS |\✔✔alpha-ketogluterate |
dehydrogenase alpha-ketoglutarate |--> |\Succinyl |\CoA |+ |*NADH* |+ |\CO TCA |\Cycle |\Step |\ 5 |- |\CORRECT |\ANSWERS |\✔✔Succinate |\thiokinase Succinyl |\CoA |--> |\Succinate |+ |*GTP* -cleaves |\high |\energy |\thioester |\bond |(S-CoA) |\to |\drive |\reaction |
forward TCA |\Cycle |\Step |\ 6 |- |\CORRECT |\ANSWERS |\✔✔succinate |
dehydrogenase succinate |--> |\fumarate |+ |*FADH2*
TCA |\Cycle |\Step |\ 8 |- |\CORRECT |\ANSWERS |\✔✔malate |\dehydrogenase L-Malate |--> |\Oxaloacetate |+ |*NADH* Direction |\of |\electron |\flow |\in |\electron |\transport |\chain |- |\CORRECT |
ANSWERS |\✔✔from |\compounds |\with |\lower |\redox |\potentials |\to |
compounds |\with |\higher |\redox |\potentials |(low |\free |\energy |\to |\high |
free |\energy) |\which |\is |\used |\to |\move |\protons |\from |\the |\matrix |\into |
the |\inter |\membrane |\space |\to |\generate |\the |\chemiosmotic |\gradient ATP |\synthase |\activity |- |\CORRECT |\ANSWERS |\✔✔Flow |\of |\protons |\back |
into |\the |\matrix |\causes |\movement |\within |\the |\enzyme |\that |\creates |
kinetic |\energy |\which |\cause |\the |\beta |\subunits |\to |\cycle |\between |\ 3 |
conformational |\states |\to |\bind |\ADP |\to |\Pi. |\Proton |\motive |\force |
provides |\the |\energy |\to |\allow |\it |\to |\cycle |\and |\release |\ATP. NADH |\and |\FADH2 |\difference |- |\CORRECT |\ANSWERS |\✔✔- |\NADH |
produces |\ 3 |\ATP |\as |\its |\electrons |\are |\passed |\to |\complex |\ 1 |\and |
FADH2 |\produces |\ 2 |\ATP |\as |\its |\electrons |\are |\passed |\to |\complex |\ 2 |
(pumps |\fewer |\protons)
- |\Only |\NADH |\produced |\locally |\can |\produce |\ 3 |\ATP |\as |\the |\inner |
mitochondrial |\membrane |\lacks |\an |\NADH |\transporter |\and |\therefore |
its |\electrons |\use |\two |\shuttle |\systems |\in |\the |\cytoplasm
Lock |\and |\key |\hypothesis |- |\CORRECT |\ANSWERS |\✔✔explains |\the |
specificity |\of |\the |\binding |\of |\substrate |\but |\not |\for |\transition |\state |
stabilization |\or |\how |\the |\enzyme |\catalyzes |\a |\reaction Induced |\fit |\model |- |\CORRECT |\ANSWERS |\✔✔Change |\in |\the |\shape |\of |
an |\enzyme's |\active |\site |\that |\enhances |\the |\fit |\between |\the |\active |
site |\and |\its |\substrate Are |\enzymes |\reversible? |- |\CORRECT |\ANSWERS |\✔✔They |\are! |\They |
work |\in |\both |\directions. |\They |\try |\to |\have |\significant |\amounts |\of |
product |\and |\reactant |\at |\one |\time. What |\are |\isozymes? |- |\CORRECT |\ANSWERS |\✔✔different |\enzymes |\that |\catalyze |\same |\reaction Gibbs |\free |\energy |(delta |\G |\value) |- |\CORRECT |\ANSWERS |\✔✔- |
negative |= |\spontaneous |\
- |\Positive |= |\require |\additional |\energy |\
- |\ 0 |= |\equilibrium What |\are |\allosteric |\enzymes? |- |\CORRECT |\ANSWERS |\✔✔- |\Have |
multiple |\active |\sites |\and |\distinct |\regulatory |\sites |\that |\control |\the |
flux |\of |\substrates |\through |\a |\biochemical |\pathway
- |\Are |\regulated |\by |\products |\of |\the |\pathways |\that |\they |\control |\and |
regulate |\the |\committed |\step |\of |\the |\pathway Allosteric |\enzyme |\regulation |- |\CORRECT |\ANSWERS |\✔✔- |\regulated |\by |\effectors |\which |\bind |\to |\allosteric |\sites |\on |\the |\enzyme - |\allosteric |\site |\is |\a |\binding |\site |\located |\away |\from |\the |\active |\site |
but |\itself |\can |\be |\another |\active |\site Homotropic |\effectors |- |\CORRECT |\ANSWERS |\✔✔- |\substrates |\for |\the |
enzyme |\and |\will |\affect |\the |\enzymes |\other |\active |\sites' |\affinity |\to |
bind |\the |\substrate - |\are |\normally |\positive |(hemoglobin's |\ability |\to |\bind |\multiple |
oxygens) Heterotropic |\effectors |- |\CORRECT |\ANSWERS |\✔✔- |\Different |\from |\the |
enzyme's |\substrate |\ - |\Often |\are |\downstream |\product |\of |\the |\pathway |\the |\enzyme |\is |
involved |\with Rate |\of |\reaction |\is |\proportional |\to |- |\CORRECT |\ANSWERS |\✔✔the |
enzyme |\substrate |\complex Michaelis-Menten |\equation |- |\CORRECT |\ANSWERS |\✔✔v0 |= |(Vmax |
[S])/(Km |+ |[S])
- |\No |\change |\to |\Vmax Uncompetitive |\inhibitors |- |\CORRECT |\ANSWERS |\✔✔- |\Bind |\to |\the |
enzyme |\when |\its |\active |\site |\is |\occupied |\ - |\Bind |\to |\allosteric |\site |\
- |\Lowers |\Km |\and |\Vmax _ |"U"niversally |\lower Noncompetitive |\inhibitors |- |\CORRECT |\ANSWERS |\✔✔- |\bind |\to |\the |
enzyme |\and |\enzyme |\substrate |\complex |\equally |\well |\ - |\Bind |\to |\an |\allosteric |\site
- |\decrease |\Vmax |\
- |\no |\change |\to |\Km Four |\major |\tissues |\that |\play |\a |\role |\in |\energy |\metabolism |- |
CORRECT |\ANSWERS |\✔✔Liver, |\Adipose, |\Muscle |\and |\Brain |\ - |\integration |\of |\energy |\metabolism |\is |\controlled |\by |\two |\peptide |
hormones: |\insulin |\and |\glucagon Insulin |- |\CORRECT |\ANSWERS |\✔✔An |\anabolic |\hormone |\produced |\by |
the |\pancreas |\ - |\stimulates |\synthesis |\of |\new |\proteins, |\fats |\and |\carbohydrates |\and |
storage |\of |\energy
Glucagon |- |\CORRECT |\ANSWERS |\✔✔- |\A |\catabolic |\hormone |\released |
by |\the |\pancreas |\that |\stimulates |\catabolic |\pathways |\
- |\Make |\stored |\energy |\available ATP |\structure |- |\CORRECT |\ANSWERS |\✔✔Adenosine, |\ribose |\and |\ 3 |
phosphates |\ - |\GTP |\is |\identical |\just |\with |\guanosine |\instead |\of |\adenosine ATP |\energy |- |\CORRECT |\ANSWERS |\✔✔Standard |\free |\energy |\stored |
between |\2nd |\and |\3rd |\phosphates |\of |\ATP |\is |-7.3kcal/mol |\ - |\same |\for |\the |\1st |\and |\2nd |\phosphates Mitochondria |\structure |- |\CORRECT |\ANSWERS |\✔✔Outer |\membrane |\is |\permeable, |\but |\the |\inner |\membrane |\is |\especially |\impermeable |\to |
allow |\the |\chemiosmotic |\proton |\gradient |\to |\form Nucleotide |\structure |- |\CORRECT |\ANSWERS |\✔✔ 5 |\carbon |\sugar |
(ribose |\or |\deoxyribose), |\phosphate, |\nitrogenous |\base |\ - |\If |\the |\structure |\does |\not |\have |\a |\phosphate |\group |\then |\it |\is |\a |
nucleoside Mononucleotides |- |\CORRECT |\ANSWERS |\✔✔are |\unbound |\to |\other |
nucleotides |\and |\can |\have |\one, |\two |\or |\three |\phosphate |\groups
gel |\electrophoresis |- |\CORRECT |\ANSWERS |\✔✔Procedure |\used |\to |
separate |\and |\analyze |\DNA |\fragments |\by |\charge |\by |\placing |\a |
mixture |\of |\DNA |\fragments |\at |\one |\end |\of |\a |\porous |\agarose |\or |
polyacrylamide |\gel |\and |\applying |\an |\electrical |\voltage |\to |\the |\gel DNA |\cloning |- |\CORRECT |\ANSWERS |\✔✔- |\used |\to |\isolate |\a |\DNA |
sequence |\and |\introduce |\it |\into |\a |\cell |\to |\amplify |\that |\DNA |\sequence
- |\Cloned |\DNA |\can |\be |\expressed |\for |\protein |\or |\used |\for |\other |\DNA |
cloning |\experiments, |\isolated |\and |\analyzed DNA |\probe |- |\CORRECT |\ANSWERS |\✔✔- |\single |\stranded |\DNA |
molecules |\that |\are |\labelled |\with |\radioisotopes |\or |\non-radioactive |
labels |\ - |\have |\sequences |\complimentary |\to |\the |\target |\DNA |\
- |\Allele |\specific |\oligonucleotides |\can |\be |\designed |\to |\bind |\to |\only |
one |\version |\of |\an |\allele - |\can |\be |\used |\for |\allele |\specific |\PCR Blotting |- |\CORRECT |\ANSWERS |\✔✔- |\transfer |\of |\macromolecules, |\such |\as |\nucleic |\acids |\or |\proteins |\to |\a |\solid-phase |\membranous |\support
- |\fragments |\of |\DNA |\and |\RNA |\molecules |\separated |\by |\gel |
electrophoresis |\based |\on |\size |\are |\blotted |\onto |\nylon |\or |
nitrocellulose |\membrane |
(SNOW |- |\DROP)
Polymerase |\Chain |\Reaction |- |\CORRECT |\ANSWERS |\✔✔- |\used |\to |
amplify |\a |\selected |\DNA |\sequence |\
- |\generate |\millions |\to |\billions |\of |\copies |\of |\a |\specific |\nucleotide |
sequence |\in |\2-3 |\hours |\ - |\requires |\single |\stranded |\DNA |\primers |\specific |\to |\the |\DNA |\of |
interest, |\DNA |\polymerase, |\dNTP |\nucleotides, |\magnesium, |\and |\the |
DNA |\to |\be |\amplified |\in |\a |\buffer - |\uses |\a |\thermocycler |\
- |\Used |\for |\forensic |\analysis |\of |\DNA |\samples, |\compare |\normal |\gene |
to |\mutant |\form |\of |\gene |\and |\detection |\of |\low |\abundance |\nucleic |
acid |\sequences Microarrays |- |\CORRECT |\ANSWERS |\✔✔- |\compare |\a |\large |\number |\of |
samples |\simultaneously - |\Contain |\thousands |\of |\immobilized |\DNA |\sequences |\on |\a |\chip |\
- |\DNA |\microarrays |\used |\to |\genotype, |\cDNA |\microarrays |\used |\for |
gene |\expression |\analysis |\ - |\can |\be |\designed |\to |\locate |\mutation |\in |\gene |\or |\to |\look |\for |
multiple |\single |\nucleotide |\polymorphisms |\in |\a |\genome CRISPR-Cas9 |- |\CORRECT |\ANSWERS |\✔✔- |\can |\directly |\edit |\human |
genome |\of |\a |\cell |\for |\a |\specific |\sequence |\
SDS-Polyacrylamide |\Gel |\Electrophoresis |- |\CORRECT |\ANSWERS |\✔✔- |
proteins |\are |\separated |\by |\size |\using |\polyacrylamide |\gels |\with |\a |
detergent |\called |\sodium |\dedecyl |\sulphate |(SDS)
- |\smaller |\proteins |\migrate |\more |\quickly |\through |\the |\gel |\
- |\allows |\for |\measurement |\of |\size |\of |\proteins Antibodies |- |\CORRECT |\ANSWERS |\✔✔- |\used |\for |\protein |\detection |\
- |\high |\specificity |\for |\their |\respective |\antigens Western |\Blots |- |\CORRECT |\ANSWERS |\✔✔- |\probe |\for |\protein |\
- |\take |\place |\after |\transferring |\the |\results |\of |\SDS-Page |\to |\a |
nitrocellulose |\or |\PVDF |\membrane |\ - |\use |\antigen |\specific |\enzyme |\labelled |\antibody |\which |\generates |\a |
band |\at |\the |\position |\of |\the |\antigen |\ - |\bands |\are |\used |\to |\determine |\the |\presence |\and |\size |\of |\protein Enzyme |\Linked |\Immunosorbent |\Assay |(ELISA) |- |\CORRECT |\ANSWERS |
✔✔- |\ 96 |\well |\microplane |\assay |\technique |\used |\to |\quantify |\protein |
expression |\and |\detect |\for |\protein-protein |\or |\protein-antigen |
interactions - |\many |\applications |\in |\research |\and |\clinically |\
- |\often |\used |\to |\detect |\immune |\responses |\for |\the |\diagnosis |\of |
disease |\and |\verification |\of |\vaccination |\
- |\Direct: |\wells |\are |\coated |\directly |\with |\antigen |\of |\interest |\which |\is |
used |\for |\blood |\samples |\and |\vaccination |\verification - |\Sandwich: |\assay |\is |\coated |\with |"capture" |\antibody |\and |\samples |
with |\unknown |\amount |\of |\antigen |\are |\added |\and |\an |\enzyme |
labelled |\antibody |\against |\the |\antigen |\is |\added |\for |\detection |\ - |\Western |\blots |\and |\ELISAs |\are |\used |\to |\confirm |\each |\other electrostatic |\interactions |- |\CORRECT |\ANSWERS |\✔✔Interactions |
between |\positively |\and |\negatively |\charged |\molecules |\attract Molecular |\dipoles |- |\CORRECT |\ANSWERS |\✔✔dipole |\moments |\allow |
molecules |\to |\align |\opposite |\to |\each |\other |\to |\maximize |\their |
electrostatic |\interactions Polar |\molecules |- |\CORRECT |\ANSWERS |\✔✔molecules |\with |\large |
dipole |\moments Hydrogen |\bonds |- |\CORRECT |\ANSWERS |\✔✔most |\important |\non |
covalent |\interaction |\as |\they |\help |\determine |\the |\structure |\and |
function |\of |\many |\molecules Hydrophobic |\effect |- |\CORRECT |\ANSWERS |\✔✔water |\forms |\an |
ordered |\cage/"shell" |\around |\the |\hydrophobic |\molecules |\and |\the |
hydrophobic |\molecules |\will |\spontaneously |\associate |\together
Basic |\amino |\acids |- |\CORRECT |\ANSWERS |\✔✔interact |\with |\negative |
molecules Aromatic |\side |\chain |\amino |\acids |- |\CORRECT |\ANSWERS |\✔✔very |\large |\and |\can |\cause |\steric |\hindrance. |\Gain |\or |\loss |\of |\these |\can |\cause |
deformities |\in |\the |\protein |\structure. Chirality |\of |\amino |\acids |- |\CORRECT |\ANSWERS |\✔✔except |\glycine, |
alpha |\carbon |\has |\ 4 |\different |\groups |--> |\chiral post-translational |\modifications |- |\CORRECT |\ANSWERS |\✔✔protein |
folding- |\chaperones |\assist |\in |\finding |\proper |\shape
- |\disulphide |\bonds |\form |\between |\thiol |\groups |\of |\cysteine |\which |
help |\stabilize |\the |\folded |\protein |\making |\it |\resistant |\to |\denaturation |\ - |\Glycosylation |\is |\a |\carbohydrate |\is |\covalently |\attached |\to |\a |\protein |
(can |\be |\added |\to |\amide |\group |\in |\asparagine |\or |\to |\hydroxyl |\group |
in |\serine |\or |\threonine |\ - |\Phosphorylation |\is |\the |\addition |\of |\phosphate |\to |\hydroxyl |\group |\in |\serine, |\threonine |\and |\tyrosine |\and |\is |\used |\to |\turn |\on |\or |\off |
proteins |\and |\enzymes sickle |\cell |\anemia |- |\CORRECT |\ANSWERS |\✔✔aggregation |\of |
hemoglobin |\within |\the |\red |\blood |\cells |\which |\results |\from |
substitution |\of |\glutamic |\acid |\to |\valine
Buffers |- |\CORRECT |\ANSWERS |\✔✔molecules |\that |\make |\solutions |
resistant |\to |\changes |\in |\pH |\when |\a |\strong |\acid |\or |\base |\is |\added |
within |\one |\pH |\unit |\above |\or |\below |\their |\pKa Zwitterionic |\form |- |\CORRECT |\ANSWERS |\✔✔one |\part |\of |\amino |\acid |\is |\positively |\charged |\and |\the |\other |\part |\is |\negatively |\charged Biological |\buffers |- |\CORRECT |\ANSWERS |\✔✔protect |\the |\body |\from |
pH |\changes bicarbonate |\buffer |\system |- |\CORRECT |\ANSWERS |\✔✔When |\pH |
decreases |\in |\the |\blood, |\bicarbonate |\buffers |\the |\change |\by |\binding |
free |\protons |(H+) |\to |\become |\carbonic |\acid, |\which |\is |\then |\further |
converted |\to |\carbon |\dioxide |\and |\water. |\When |\the |\pH |\increases |
carbonic |\acid |\buffers |\the |\change |\through |\releasing |\its |\proton |\and |
becoming |\bicarbonate Primary |\structure |- |\CORRECT |\ANSWERS |\✔✔linear |\sequence |\of |
amino |\acids |\with |\the |\absence |\of |\R |\group |\interactions. |\This |\is |
determined |\by |\the |\DNA |\blueprint. |\N |\terminal |\on |\left, |\C |\terminal |\on |\the |\right. Secondary |\structure |- |\CORRECT |\ANSWERS |\✔✔Is |\the |\folding |\of |\the |
amino |\acid |\chain |\specific |\patterns. |\Maximal |\hydrogen |\bonding |\is |
the |\goal. |\Formed |\into |\alpha |\helices |\and |\beta |\sheets.
quartenary |\structure |- |\CORRECT |\ANSWERS |\✔✔two |\or |\more |
polypeptides |\interact |\to |\form |\a |\functional |\protein Alzheimer's |\disease |- |\CORRECT |\ANSWERS |\✔✔abnormal |\cleave |\of |\the |\amyloid |\precursor |\protein |\in |\the |\brain. |\New |\protein |\adopts |\beta |
sheet |\structure |\and |\forms |\plaques. |\It |\is |\a |\neurotoxin. Prion |\disease |- |\CORRECT |\ANSWERS |\✔✔Proteins |\are |\able |\to |\fold |\in |
multiple |\distinct |\different |\structures |\and |\one |\form |\can |\cause |\other |
PrP |\proteins |\to |\fold |\into |\the |\same |\form. |\Alpha |\helices |\are |\refolded |
into |\beta |\sheets |\into |\an |\infectious |\form |\and |\is |\resistant |\to |
degradation |\and |\accumulates.
