Term
Enzymes are neither _____ nor _______ during reactions, because they are biological __________. |
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Definition
formed, consumed, catalysts |
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Term
Most enzymes are _________, but some are ______ _______ such as __________. |
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Definition
proteins, nucleic acids, rRNA |
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Term
Enzymes significantly enhance the rate of reactions, by sometimes as much as ______. |
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Definition
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Term
What enzyme catalyzes the dissociation of CO2 in H2O? |
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Definition
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Term
Even though this reaction can occur spontaneously, how much faster does dissociation of CO2 in H2O happen in the presence of its catalyst? |
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Definition
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Term
What value/unit of measure is used to rate the efficiency or productivity of an enzyme? |
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Definition
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Term
What units does turnover number use? |
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Definition
How many molecules of reactant an enzyme can convert to product per second |
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Term
What is a proteolytic enzyme? |
|
Definition
An enzyme that cleaves peptide bonds |
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Term
DNA polymerase has an error rate of? |
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Definition
1 out of every 10^8 base pairs - very specific recognition capability |
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Term
What is one characteristic about substrates that allows enzymes to be so specific? |
|
Definition
substrate stereochemistry - enzymes are stereospecific in that they often only recognize L conformers, and ignore D conformers |
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Term
What is one way enzyme activity is regulated? |
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Definition
Activation - many enzymes are produced in their inactive form and must be activated by some other mechanism |
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Term
What is the inactive form of Trypsin? |
|
Definition
Trypsinogen - another enzyme cleaves a specific peptide bond, cutting trypsin into two parts, making one of the newly formed polypeptides an active form of trypsin |
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Term
What is covalent modification used for? |
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Definition
Regulation of enzyme activity |
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Term
Phosphorylation can either _______ or _______ enzyme activity, depending on the enzyme's conformation. |
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Definition
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Term
What functional group among amino acids is often phosphorylated in order to regulate enzyme activity? |
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Definition
-OH groups - tyrosine, serine, and threonine |
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Term
What is feedback inhibition? |
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Definition
Regulation of enzyme activity by the resultant product of the enzyme's activity coming and binding to the enzyme when the product is in excess, thereby inhibiting the enzyme's activity |
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Term
Reversible inhibition falls into two types: |
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Definition
Competitive and noncompetitive |
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Term
What is competitive inhibition? |
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Definition
a molecule that is structurally similar that binds to the active site in an enzyme, "competing" for the active site with the substrate, thus inhibiting the enzyme from forming product |
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Term
What is noncompetitive inhibition? |
|
Definition
a molecule that binds to a site on an enzyme that is not on the active site. so, regardless of whether the substrate concentration is in excess or not, the enzyme's activity is inhibited |
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Term
Which kind of inhibition can be remedied by increasing substrate concentration? |
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Definition
Competitive - if the mechanism acts competitively, then the molecule that is most concentrated will beat out the inhibitor substrate and thus the inhibition will be rememdied and enzyme activity will be restored |
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Term
What is a competitive inhibitor for the succinate ion? |
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Definition
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Term
How does sulfanilamide work? |
|
Definition
competitive inhibitor for an enzyme in bacteria that converts PABA into folic acid, thereby retarding bacterial growth. this does not affect mammals (hosts) b/c mammals absorb folic acid through their diets |
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Term
How is effectiveness increased in competitive inhibition when synthesizing antibiotics? |
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Definition
greater diversity - bacteria reproduce very quickly, so they are able to mutate and survive antibiotic treatment. so, providing greater diversity puts up roadblocks for mutations that will allow bacteria to survive |
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Term
How does methotrexate work? |
|
Definition
binds 1000-fold more tightly (competitive inhibition) than tetrahydrofolate, the normal substrate, to the dihydrofolate reductase, which assists in the biosynthesis of purines and pyrimidines. it reduces nucleotide synthesis, and thus it inhibits DNA replication and can help treat cancer |
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Term
What is tetrahydrofolate? |
|
Definition
it is the normal substrate for dihydrofolate reductase, the enzyme that assists in purine and pyrimidine synthesis, thus facilitating DNA replication by providing new nucleotide bases |
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Term
|
Definition
the Km of a competitive inhibitor for a given enzyme |
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Term
The lower the Km value, the greater the _________ for enzymes and substrates. |
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Definition
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Term
The higher the Km value, the lower the ___________ for an enzyme and substrate. |
|
Definition
affinity - Km and enzyme affinity for substrate have an inverse relationship |
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Term
What is an experimental way of determining whether an inhibitor is competitive or noncompetitive? |
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Definition
if a sample has a given amount of enzyme, then adding a given amount of inhibitor, by adding an increasing amount of substrate will tell you which - if Vmax can be achieved, then the inhibitor is competitive. if it is noncompetitive, then Vmax cannot be attained. |
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|
Term
How do irreversible inhibitors [often] bind to enzymes? |
|
Definition
they make covalent linkages to amino acids at the active site in the enzyme - this is toxic to the cell |
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Term
|
Definition
diisopropylphosphofluoridate - has a F substituted for an -OH group on a phosphate, making it highly reactive - forms an ester linkage with a serine |
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Term
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Definition
makes covalent linkage to cysteine residues |
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Term
How does penicillin work? |
|
Definition
irreversible inhibitor that acts on bacterial transpeptidase. |
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Term
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Definition
strengthens bacterial walls by forming peptide bonds between D-amino acids that cross link peptidoglycan structure, facilitating cell growth. so, if you inactive this enzyme, then the cell cannot grow and divide |
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|
Term
Why does penicillin not kill mammallian cells? |
|
Definition
because MOST of our amino acids are the L enantiomer and the bacterial are D enantiomers |
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Term
Penicillin contains a beta-_______ ring (cyclic amide) fused to a ___________ ring. |
|
Definition
lactam, thiazolidine - the 4-membered ring in the beta-lactam is highly reactive |
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Term
Penicilan forms what kind of linkage with what amino acid in the active site? |
|
Definition
ester linkage, nucleophilic attack, serine |
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Term
What was the first penicillin that was stable in acidic conditions, and thus able to withstand oral ingestion? |
|
Definition
Penicillin V - has a phenoxymethyl group on it - resonance stabilization |
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|
Term
What does PenVK stand for? |
|
Definition
Penicillin V, Potassium salt - the COOH group gets a K+ associated with the O-, making it more soluble |
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Term
If you have an allergy to penicillin, are you able to take any other "cillins"? |
|
Definition
no, if the person has an allergy to the beta-lactam ring or any other aspect of the "cillin" part of the antibiotic, then they cannot take it. |
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|
Term
Enzymes utilize what 4 rxns for catalysis? |
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Definition
acid/base, covalent, metal ion, alignment (approximation) |
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Term
Additional free energy is obtained through the _______? |
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Definition
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|
Term
How can enzyme mechanisms be "visualized"? |
|
Definition
X-ray crystallography/NMR, and chemical modification of active sites gives insight to what groups participate |
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Term
Genetically engineered enzymes can be used for what? |
|
Definition
chemical modification for enzyme mechanism "visualization" |
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Term
Lysozymes use what kind of catalysis? |
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Definition
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|
Term
Carbonic anhydrase uses what kind of catalysis? |
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Definition
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|
Term
Lysozyme acts by cleaving _____________ that give structural integrity to bacterial cell walls |
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Definition
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Term
Cell wall polysaccharides are composed of two kinds of glucose derivatives connected by what? |
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Definition
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Term
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Definition
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Term
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Definition
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Term
Chitin has what kind of polysaccharide beta 1-4 linkage? |
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Definition
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|
Term
What type of interaction brings the NAG-NAM hexamer into the active site of the enzyme? |
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Definition
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|
Term
Between what two sites of the NAG-NAM hexamer is the molecule cleaved? |
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Definition
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|
Term
How does an enzyme's active site have a different pH than physiologic pH? |
|
Definition
A microenvironment is created, so isolated regions of the enzyme may have different pH, allowing for protonation of some residues and not others |
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Term
the enzyme cleaves the D-E NAG-NAM bond by __________ ________ on the -0H of the active site, deprotonating the -OH on the enzyme and donating that proton to the E residue, making it a leaving group |
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Definition
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|
Term
Optimum pH for Lysozyme is? |
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Definition
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|
Term
AT a pH>5, Glu-35 ______ and cannot supply the hydrogen ion required for cleavage |
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Definition
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Term
For carbonic anhydrase, the limiting factor is what? |
|
Definition
how fast the substrate (CO2 and H20) can diffuse into the active site (demonstrating how fast and efficient this enzyme is) |
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Term
WHat metal cofactor helps water prepare for formation of carbonic acid? |
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Definition
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|
Term
Zinc reduces the pKa for water from 15.7 to what? |
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Definition
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|
Term
The 3 residues bound to the Zinc in carbonic anhydrase are what? |
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Definition
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|
Term
What residue on carbonic anhydrase shuttles the build-up of H+ ions in bicarb formation? |
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Definition
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|
Term
Serine proteases act in what manner to cleave bonds? |
|
Definition
as strong nucleophiles attacking carbonyl carbon in peptide bonds - (the OH on the functional group) |
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Term
|
Definition
catalyzes the hydrolysis of peptide bonds following amino acids with large, bulky nonpolar groups (no charge) hence its lack of specificity |
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|
Term
Chymotrypsin can be tricked into hydrolyzing a synthetic substrate that releases a highly colored substrate such as what? |
|
Definition
p-nitrophenol - for study in the lab |
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|
Term
For chymotrypsin, Ser-195 attacks substrates forming what kind of linkage? |
|
Definition
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|
Term
After Ser-195 forms an ester linkage to a substrate, water enters and does what? |
|
Definition
deacylates the enzyme by hydrolyzing the ester bond |
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|
Term
For chymotrypsin's action, which step of the reaction is rate-limiting? |
|
Definition
hydrolysis of the ester bond |
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Term
How was the rate-limiting step determined for chymotrypsin? |
|
Definition
Burst-phase kinetics = once all enzymes have been acylated, they wait for water to release the substrate and this can be measured with special instruments |
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|
Term
In burst phase kinetics, increasing the enzyme and substrate concentration will produce what on the absorbance plot? |
|
Definition
a steeper and longer burst phase, but once they are all acylated, then the steady state is again attained |
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Term
For the serine in chymotrypsin, how do you achieve a stronger nucleophile? |
|
Definition
the carboxyl group is negatively charged, drawing the h- off of the histidine, and then the histidine draws the h- off of the hydroxyl group of the serine. thus, resonance provides a more negative charge on the hydroxyl (alkoxide if fully deprotonated), making it a stronger nucleophile |
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|
Term
for chymotrypsin, once the resonance form has made the alkoxide on the serine (making a stronger nucleophile), then what happens? |
|
Definition
the alkoxide oxygen reaches for the carbonyl carbon of a substrate, making an ester linkage (nucleophilic attack) |
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|
Term
the newly formed enzyme-substrate anion is called what for chymotrypsin? |
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Definition
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|
Term
what does the production of an oxyanion achieve in catalysis in chymotrypsin? |
|
Definition
lowered energy of activation |
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|
Term
BE ABLE TO DRAW SLIDE 34 OF ENZYME MECHANISMS |
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Definition
BE ABLE TO DRAW SLIDE 34 OF ENZYME MECHANISM |
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|
Term
How do different serine proteases (having the same mechanism) have different specificities? |
|
Definition
a separate "pocket" with different amino acid side chains providing the diversity |
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|
Term
how do chymotrypsin and trypsin differ? |
|
Definition
chymotrypsin has just the serine providing for specificity, whereas trypsin has an asp-189 with a negative charge, attracting positively charged substrates (arginine and lysine) |
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|
Term
Where are chymotrypsin and trypsin synthesized? |
|
Definition
pancrease - inactive form |
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|
Term
|
Definition
a serine protease that is synthesized and stored in an inactive form in high concentrations in granules until they are summoned by the body |
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Term
What is the inactive precursor to chymotrypsin/trypsin? |
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Definition
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|
Term
Crystalline, inactivity, and storage in granules are they body's mechanism for what? |
|
Definition
protecting our tissues from enzymatic attack |
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|
Term
pi-chymotrypsin does what to activate trypsin? |
|
Definition
binds to inactive chymotrypsinogen and cleaves it between 15 and 16 residues |
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|
Term
What is a 4th way that the body protects itself from proteolytic attack on its own tissues? |
|
Definition
synthesizing competitive inhibitors |
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|
Term
How does the body's competitive inhibitor inhibit serine proteases? |
|
Definition
it turns the histidine out of plane, impeding the flow of electrons forming resonance structures, so the alkoxide ion cannot form, inactivating the serine residue. |
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|
Term
Upon entering the duodenum, how is the inhibitor removed from the serine protease? |
|
Definition
dilution causes it to dissociate from the enzyme |
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|
Term
|
Definition
type Z mutation in elastase inhibitor - lys substitutes for glu-53. |
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Term
What do elastase inhibitors do? |
|
Definition
prevent elastase enzymes from digesting alveolar proteins in the lungs |
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Term
|
Definition
z-mutation in elastase inhibitor |
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Term
What do enzymatic cascades serve to do? |
|
Definition
amplify a cellular signal |
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Term
What is an example of enzymatic cascade utilizing the consequential amplification? |
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Definition
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|
Term
Aldoses and ketoses of appropriate lengths can cyclize forming what two rings? |
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Definition
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Term
Aldehydes form what kind of linkages? |
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Definition
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Term
Ketoses form what kind of linkages? |
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Definition
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Term
The number 5 carbon in carbohydrate rings, this carbon is the what? |
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Definition
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Term
Ketose sugars are capable of rearranging their structures into aldoses via what mechanism? |
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Definition
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Term
When ketose and aldose forms of sugars are in equilibrium, which form predominates? |
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Definition
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Term
What is another term for ketoses? |
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Definition
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Term
Sugars with aldehyde groups (or potential aldehydes) are called what? |
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Definition
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Term
Reducing sugars can reduce what (with blue solution) to what and is the basis for what test? |
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Definition
Cu2+ to Cu1+ (insoluble red precipitate) - Benedicts test |
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Term
What is Fehling's solution used for? |
|
Definition
the benedict's test - testing for reducing sugars |
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Term
Manitol, sorbitol, and other things like this are examples of what? |
|
Definition
sugar alcohols - aldoses that have been reduced to sweeten products that we consume |
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Term
What is the term for carbohydrates that are locked into their cyclic form (cannot open the ring preventing aldehyde formation)? |
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Definition
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|
Term
What is the difference between hemiacetal and acetal linkages? |
|
Definition
C-O-C-OH (hemiacetal) vs. C-O-C-O-CH3 (acetal) |
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|
Term
How is a nonreducing sugar produced? |
|
Definition
by making an acetal group where otherwise a hemiacetal group would be present, locking the ring into ring form |
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Term
What two unique items are present in heparin polymers? |
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Definition
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Term
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Definition
prevents thrombin from converting fibrinogen into fibrin, so it is a anticoagulant |
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Term
Sucrose is formed by what? is it a reducing sugar? |
|
Definition
a glycosidic linkage alpha(1-2) linkage between glucose and fructose - thus, it is NOT a reducing sugar |
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Term
Lactose is what kind of linkage? |
|
Definition
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|
Term
The most common polysaccharide in animal cells is what? |
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Definition
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|
Term
Glycogen is a polymer of glucose, containing both _______ and ______ linkages at branch points |
|
Definition
alpha (1-4) and alpha (1-6) |
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Term
Branching occurs about every ______ glucose molecules in glycogen |
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Definition
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|
Term
The hemiacetal at the #1 carbon in the first monomer of the polymer of glycogen is significant because why? |
|
Definition
it is the only reducing sugar in the whole polymer |
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Term
Starch is also called what? |
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Definition
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|
Term
Amylose is a what kind of polysaccharide? |
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Definition
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|
Term
The branched form of amylose is called what? |
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Definition
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|
Term
Amylopectin has a lower degree of branching, occurring at a rate of 1 out of every _____ glucose residues. |
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Definition
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|
Term
Fruits are gassed with what to prevent ripening? |
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Definition
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|
Term
Once fruit has arrived at its destination, it is then gassed again with what to promote ripening? |
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Definition
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|
Term
Methylcyclopropene is what with regard to fruit ripening? |
|
Definition
a competitive inhibitor for the ethylene that ordinarily promotes ripening |
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Term
In aqueous solutions, starch molecules take what shape? |
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Definition
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|
Term
Starch's helical structure in solution accommodates what into its color causing a color change to blue/black? |
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Definition
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|
Term
What enzyme catalyzes starch in the food that we consume in the saliva? |
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Definition
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|
Term
Amylase catalyzes the hydrolysis of what bonds? |
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Definition
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|
Term
Starch -> ___________ -> maltose -> ____________? |
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Definition
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|
Term
Partially __________ starches are more soluble than starch. |
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Definition
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|
Term
Mixtures of what and what are used in baby foods and infant formulas? |
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Definition
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|
Term
The large size of glycogen prevents what? |
|
Definition
the glycogen molecules from diffusing out of the cells |
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|
Term
Storage of glycogen reduces _______ pressure? |
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Definition
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|
Term
When glycogen becomes highly concentrated in the cell, it can __________ or ___________ into _________ __________. |
|
Definition
precipitate or crystallize, glycogen granules |
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|
Term
Cellulose is the polyglucose polysaccharide that uses what kind of linkages? |
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Definition
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|
Term
Cellulose has a much higher ________ strength than starches. |
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Definition
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|
Term
Humans cannot digest cellulose because why? |
|
Definition
We do not have an enzyme that is capable of breaking beta (1-4) linkages |
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Term
How are other animals able to digest cellulose? |
|
Definition
Symbiotic bacteria present in the gut of these animals. these bacteria do synthesize enzymes that can hydrolyze beta (1-4) linkages |
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|
Term
What do glycotransylferases do? |
|
Definition
synthesize polymeric carbohydrates |
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|
Term
In blood typing, what is the common oligosaccharide in what blood type polysaccharides? |
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Definition
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|
Term
Type A blood has what that differs from O blood? |
|
Definition
adds N-acetylgalactosamine |
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|
Term
Type B differs from type O how? |
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Definition
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|
Term
The two enzymes' primary structure for A and B blood types differs by only how many amino acids? |
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Definition
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|
Term
Some microorganisms utilize specific what to bind to host cells? |
|
Definition
specific carbohydrate structures |
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Term
Influenza viruses recognizes what compound on cell surfaces of hosts? |
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Definition
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|
Term
The fat content of foods is determined by what? |
|
Definition
simple extraction (with hexane) |
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|
Term
How do you figure out fat content per serving? |
|
Definition
samples are extracted in hexane for extended periods of time. the hexane is then separated from the food and then the hexane is evaporated off. the mass of residual materials is collectively called the fat content |
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|
Term
lipids can be broken down into two different categories called what? |
|
Definition
saponifiable and non saponifiable |
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Term
Steroids and prostaglandins are what categorization of lipids? |
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Definition
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|
Term
________ _______ are the primary component of lipids. |
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Definition
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Term
Almost all double bonds in naturally occuring fatty acids are in the ______ configuration. |
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Definition
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|
Term
The IUPAC system assigns #1 to the ________ carbon of lipids |
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Definition
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|
Term
For lipids, biochemists use the greek alphabet, and the #2 carbon becomes what? |
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Definition
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Term
For lipids, the terminal carbon is always named the what? |
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Definition
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|
Term
In lipids, double bonds are often identified by their distance from what? |
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Definition
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|
Term
Why do you never have odd numbered carbon lipids? |
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Definition
b/c they are synthesized two carbons at a time |
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Term
Prostaglandins are synthesized from what acid? |
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Definition
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|
Term
Prostaglandins also promote what? |
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Definition
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|
Term
Aspirin and Ibuprofen inhibit what? |
|
Definition
the first enzyme in the inflamm. pathway, prostaglandin H2 synthetase |
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Term
The fluidity (melting points) of lipids depends upon what? |
|
Definition
chain length and degree of unsaturation |
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Term
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Definition
an emulsion of oil and water |
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|
Term
What component of margarine influences its melting point? |
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Definition
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|
Term
What is the main source of oil for margarin? |
|
Definition
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|
Term
A higher number of double bonds will do what to the texture of margarine? |
|
Definition
make it softer. fewer double bonds makes it stiffer |
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Term
Cis-configured double bonds do what to the melting points of margarine? |
|
Definition
they disrupt dipole interactions and the orderly stacking of saturated fatty acids, lowering the melting point |
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|
Term
Catalytic hydrogenation produces what? |
|
Definition
sometimes when hydrogenating a double bond, the single bond will rotate into a trans configuration, producing trans-fats |
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|
Term
The degree of unsatruation is measured by what method? |
|
Definition
titration of double bonds with molecular iodine |
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|
Term
The iodine number is the number of grams of iodine that reacts with what? |
|
Definition
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|
Term
The most common storage form of fats are what? |
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Definition
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|
Term
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Definition
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|
Term
Three fatty acids are _________ to ________, one to each alcoholic group |
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Definition
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|
Term
Most lipids found in membranes are what? |
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Definition
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|
Term
Another class of saponifiable lipids are built around what rather than glycerol? |
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Definition
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|
Term
Sphingomyelin contains a what kind of ester and a second fatty acid linked by what kind of bond? |
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Definition
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|
Term
WHich bond is saponifiable in sphingomyelin? |
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Definition
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|
Term
Cerebrosides are composed of what 3 things? |
|
Definition
sphingosine, fatty acid, and a carbohydrate |
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|
Term
Cholesterol is a lipid with an entirely different what from other lipids? |
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Definition
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|
Term
|
Definition
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|
Term
Cholesterol is composed of what 4 things? |
|
Definition
4 fused hydrocarbon rings |
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|
Term
Cholesterol is synthesized by whom? |
|
Definition
animals, not plants or prokaryotes |
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|
Term
Cholesterol is the starting material for the biosynthesis of what 3 things as examples? |
|
Definition
hormones, vitamin D, and bile salts |
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Term
Bile salts are ________ agents that help solubilize dietary lipids in the aqueous environment if the GI |
|
Definition
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|
Term
Bile is synthesized where? |
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Definition
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|
Term
Bile salts are stored where? |
|
Definition
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|
Term
Fresh bile is _______, but upon standing, it turns _______ and finally ________. |
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Definition
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|
Term
The body excretes ________ to ________ grams of bile daily and is responsible for the color of what? |
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Definition
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|
Term
Waxes (that are used to coat feathers) are what of long-chain fatty acids and fatty alcohols? |
|
Definition
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|
Term
|
Definition
sheet-like structures only two molecules thick consist of mainly lipids and proteins form spontaneously into lipid bilayers are non-covalent assemblies are asymmetric are fluid structures are electrically polarized |
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|
Term
Ionized lipids such as phospholipids spontaneously form what? |
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Definition
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|
Term
Sonication of phospholipid suspensions yield what? |
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Definition
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|
Term
How are artificial lipid vessicles formed? |
|
Definition
sonication of phospholipids |
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|
Term
How can liposomes be used to study cell behavior in different environments? |
|
Definition
They can form artificial membranes through gel filtration that can be used to study different behavior on cells in solution with different solution contents |
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|
Term
Artificial BLM stands for what? |
|
Definition
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|
Term
ABLM's can be formed how? |
|
Definition
can be formed across small millimeter-sized holes by "painting" the lipid mixture over the holes. this causes artificial BLM's form spontaneously, and then when this is complete, the bilayer looks black due to destructive interference of refracted light |
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|
Term
In making ABLM's, the bilayer looks black due to what? |
|
Definition
destructive interference of refracted light |
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|
Term
The hydrophobic nature of the middle of membranes makes them excellent barriers to what? |
|
Definition
ionic and polar molecules |
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|
Term
membrane proteins are classified by how strongly they are held by what? |
|
Definition
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|
Term
Peripheral proteins are held by what? |
|
Definition
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|
Term
The fluid mosaic model of membranes explains what? |
|
Definition
why individual lipid molecules are free to diffuse latterally across the membrane, but they cannot easily flip over |
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|
Term
What method can be used to visualize lipid molecules diffusing laterally across membranes? |
|
Definition
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Term
Bacteria regulate the fluidity of their membranes by varying the degree of what? |
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Definition
the degree of unsaturation and the length of their fatty acids |
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Term
Membrane fluidity is often characterized by their phase transition temperature, or what? |
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Definition
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Term
Prostaglandin H2 synthetase is an integral protein and is held in its membrane by a set of _____ _______ coated with _________ side chains |
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Definition
alpha helices, hydrophobic |
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Term
In Prostaglandin H2, a hydrophobic channel shuttles what into position for conversion? |
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Definition
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Term
Aspirin blocks what aspect of prostaglandin H2? |
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Definition
the channel that shuttles in arachadonic acid |
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