Biochem exam 1 gift
6. Which of the following is the [REDACTED]est interaction?
(This was in a quiz) - Strongest interaction: hydrogen bond in hydrophobic environment due to less free availability of other water molecules (hydrophobic effect). - Weakest interaction: hydrogen bond in aqueous environment, there are always available hydrogen for water to bind to.
25. What is the charge on the following peptide at standard biochemical pH?
(pH=7) C terminus has a charge of -1 at neutral/high pH and 0 at low pH (approx pka = 2) 0 to -1 at pH 3 (according to exam review) N terminus has a charge of +1 at low/neutral pH and 0 at high pH (approx pka = 10/11) +1 to 0 at pH 10 (according to exam review) All polar & non polar AA don't add any charge no matter the pH! Pka values to remember if you want: Basic amino acids = 9/10 Acidic amino acids = 5 Hisitine (special case) = 6 Standard pH= 7 Adding up charges in peptides eg. DEHRK @ pH =7 or biological pH, the answer is 0 Example: SYSFKIVFLL, pH= 7, charge = +1 see image
4. Which of the following reactions is [REDACTED] fastest? (Select all that apply)
**Image** Thermodynamic reactions explain if reaction would proceed, i.e. spontaneous reactions (doesn't give the rate of the reaction). Kinetic reactions explain the rate of the reaction, reactions with enzymes that lower the activation energy would happen faster than non enzyme reactions. If, for example, the free energies were given and the question asks which reaction is proceeding at the fastest rate, you would not be able to determine that from the information provided since dG does not tell us anything about the rate of the reaction; it only tells us if it can proceed.
1. Below two statements are provided, determine which (if any) are false: (i) At equilibrium, [REDACTED]; (ii) this means the reaction [REDACTED].
**Image** -At equilibrium, delta G is equal to zero, this means the rate of the forward reaction equals the rate of the backward reaction. -At equilibrium, delta G is equal to zero, this means the reaction's free energy=0 kcal/mol. -At equilibrium, the chemical reaction has not halted; this means the reaction absorption and release of energy are the same and no energy can be extracted from the system. -At equilibrium, the cell is dead, entropy will take over. -At equilibrium, delta G = 0; this means the reaction cannot do work. -An equilibrium reaction remains at equilibrium regardless of directionality. (i)At equilibrium, the chemical reaction has not halted; both the forward and reverse reactions are occurring at the same rate; the absorption and release of energy are the same which is why dG will equal 0 and no energy can be extracted from the system. (ii) Since at equilibrium there is no Free Energy leaving or entering the system (dG = 0), there is no energy available for work to be transferred or used elsewhere
15. Which of the following pairs is most likely formed by a polar bond?
**Image** -Polar covalent bonds, the electrons are shared unequally, as one atom exerts a stronger force of attraction on the electrons than the other. Electronegativity difference between the anion and cation is between 0.4 and 1.7. Examples: N-H, O-H, F-H -Hydrogen bonds are polar O=3.5, H=2.1 in electronegativity ex) !!! answer: H-N
21. Assuming the oligopeptide [REDACTED] forms one continuous α-helix, the [REDACTED] residue is hydrogen bonded to ... (select all that apply)
**Image** leucine & lysine
2. Which of the following statements about Entropy are correct? (Select all that apply)
-Decreased by folding a peptide into shape. -Is a measure of the number of states a system occupies. -Entropy is increased and as a result energy decreases. -Increasing entropy helps lower energy (energy is lost as heat that increases entropy). -Entropy is very important in biochemistry. -Decreasing entropy requires an input of energy. -High entropy = low E(more stable/organized) -One way entropy increases is through loss of heat energy which is vibrational energy. -Remember entropy as additional states something can occupy. -Every reaction will not be 100% (second law of thermodynamics), releasing some heat, therefore always increasing the entropy of the universe (even if an endergonic reaction). -Is NOT a measure of disorder.
5. Which of the following reactions is [REDACTED]gonic? (Select all that apply)
-Exergonic reaction= spontaneous rxn: delta G= negative, reaction releases energy, product is lower energy than reactants, catabolic/oxidative reactions (breakdown of large molecules into smaller ones) in the body are exergonic. (ex) hydrolysis -Endergonic reaction= non spontaneous rxn: delta G= positive, reaction absorbs energy, reactant is lower energy than product. Anabolic/reductive reactions (building complex molecules from smaller ones) in the body are endergonic. (ex) dehydration reaction -The reverse of a reaction has the same magnitude but opposite signs. So if a reaction (as written) is endergonic (positive delta G), then the reverse of the reaction is exergonic (negative delta g)
18. Given the respiration / blood buffering system shown, select the correct statement.
-The blood buffering system maintains the pH of blood near 7.34 -The blood buffering system utilizes the H2CO3/HCO3- conjugate acid/base pair. -The blood buffering system is facilitated by the enzyme anhydrase, which interconverts carbon dioxide and water to carbonic acid, ionizing into bicarbonate and H+. -Hyperventilation causes the CO2 to decrease, hypoventilation causes the CO2 in your body to increase -Hyperventilation causes decrease in proton (more proton absorbed) and pH increases -During hyperventilation, the system will need to increase bicarbonate - hypoventilation causes increase in proton and pH decreases - hypoventilation = blood becomes more acidic - hyperventilation = blood becomes more basic
23. What is the particular characteristic that peptide bonds must have that distinguishes them from other amides?
A peptide bond must have planarity and resonance between the N-C-O system. Peptide bonds are rigid, planar, and flat. They do NOT rotate. It is stabilized by resonance. This resonance increases the polarity of the nitrogen and oxygen. The increase in polarity leads to hydrogen bonds that are much stronger than most other hydrogen bonds. The double bond character between the carbon and the nitrogen restricts rotation about this bond.
22. Comparing a titration curve for an unknown amino acid against the amino acid [REDACTED], which amino acid would be the closest match?
Amino acids with non-ionizable side (nonpolar/polar neutral) chains will have 2 characteristic inflection points due to ionization of carboxyl and amino groups (inflection points found at horizontal-ish sections of the graph ~2.3 and ~9.6). Amino acids with acidic or basic chains will ;/have 3 inflection points for the horizontal-ish regions, with the middle one being the point at which the side chain is ionized. For acidic AA, this middle inflection will be ~4 and for basic AA it will be ~9) Example : comparing a titration curve for an unknown amino acid against the amino acid D, which amino acid would be the closest match? E(glu) bc it's also a negative charged amino acid with 3 inflection points. Possible answers could be R,H, K if E isn't an option.
17. What is carboxylate?
Carboxylate is the conjugate base of a carboxylic acid, RCOO−. It is an ion with negative charge (anion). It will bind to the amine group of the next amino acid forming a water molecule as a leaving group, it creates a peptide bond. Carboxylate is considered a base (proton acceptor). Carboxylic acid would be the acid (proton donor).
9. Below two statements are provided, determine which (if any) are false: (i) [REDACTED] a carboxylate and a carboxylic acid are [REDACTED], (ii) they [REDACTED] different properties in aqueous solutions
First Part: -Carboxylate (strong nucleophile) is more stable than carboxylic acid because it's resonance stabilized. -Carboxylate and carboxylic acid are different structures; similar but not identical (carboxylate is the conjugate base of carboxylic a.) Second Part: they exhibit different properties in aqueous solutions. Even though a carboxylate and a carboxylic acid are similar (TRUE), they have different properties in aqueous solutions (TRUE) (i) Even though a carboxylate and a carboxylic acid are identical, (ii) they have different properties in aqueous solutions. (i) is false because carboxylates lack the hydrogen of the hydroxyl group and are represented by RCOO- while carboxylic acids have the hydrogen and are represented by RCOOH. (ii) is true
7. Below two statements are provided, determine which (if any) are false: (i) Free energy (dG) [REDACTED], (ii) however, we can anticipate the [REDACTED] reaction from its dG value.
First part: delta G=delta H -T*delta S if delta G is negative=exergonic, spontaneous. If delta G is positive=endergonic or non spontaneous. Free energy does NOT tell us the speed of the reaction Second Part: We can't anticipate the speed/kinetics of the reaction from the delta G value. Another possibility is that we can determine the rate of the reaction based on delta G. This is false. It would be We CAN anticipate whether the reaction will occur or not without outside influence from its dG value Free energy does not inform kinetics so we CANNOT anticipate the speed of a reaction from its dG value Free energy of zero has no capacity to do work. Any system that is out of equilibrium stores free energy that can be used for work EX: (i) Free energy does not inform kinetics, (ii) however, we can anticipate the speed of a reaction from its dG value. i is true and ii is false
26. Does the following sequence have an amino acid that [REDACTED] bonds?
Forms sulfur or hydrogen bonds? Hydrogen bonds are 4 amino acids away. Probably talking about sulfur bonds/bridges, only covalent bonds in 3 or 4 degree structures (methionine (can't do anything because the sulfur is stuck in the middle) and cysteine). If a sequence has 2 cysteines, then it can form a disulfide bond/bridge. Example: Can LMATYRQS make disulfide bonds? NO, because there is no cysteine( C) in the sequence. Methionine can't make a disulfide bond.
3. Which of the following forces is driven primarily by [REDACTED]?
Hydrophobic effect (attraction between two molecules that are non-polar) is primarily driven by an increase in the entropy of water molecules - when nonpolar substances are excluded, the ordered water molecules become disordered and return to the bulk solvent Delta G = negative; hydrophobic interactions are spontaneous. Hydrophobic: does not dissolve in water Hydrophilic: dissolves in water Polarity van Der Waals Forces dipole-dipole interaction Permanent dipole-induced dipole Induced dipole-dipole Imagine oil and water, polar and nonpolar molecules will not MIX therefore hydrophobic effect allows the different groups to separate and allow like molecules to stick with like molecules, allowing higher entropy and lower energy Decreasing the number of water molecules around hydrophobic groups increases the entropy of the bulk water
20. What is the charge on the [REDACTED] of [REDACTED] at pH 5?
If C terminus (approx pka= 2): -1 Has a charge of -1 at neutral/high pH and 0 at low pH If N terminus (approx pka= 9): +1 Has a charge of +1 at low/neutral pH and 0 at high pH Remember, they may ask you to compare pH to pka (they will give us pka values): If pH is MORE THAN the pka = deprotonated (-1 charge if acidic, 0 charge if basic) If pH is LESS THAN the pka = protonated (0 charge if acidic, +1 charge if basic) Pka values to remember if you want: Basic amino acids side chain = 10.5 or 12.5 Acidic amino acids side chain = 3 or 4 Histidine (special case) side chain = 6
11. A technician is examining a degradation / synthesis coupled reaction. The technician notes that the synthetic reaction requires [REDACTED] kcal/mol of energy per biomolecule synthesized. Also, the degradation reaction produces [REDACTED] kcal/mol of energy. The technician argues that this is enough energy to make [REDACTED] moles of the biomolecules. What error, if any, has the technician made in the analysis?
If the technician thinks the amount of energy produced going to make the exact # moles of product, then he/she is not considering the 2nd law of thermodynamics. Heat is escaped as energy in transfer from one form to another, greater entropy is always happening. (ex. Requires 7.14 kcal/mol...produces 21.42 kcal/mol...make 3 moles, this is breaking the second law of thermodynamics) Not breaking any law: requires 7.14 kcal/mol...28.56 kcal/mol... makes 3 moles because there is more energy than the energy it started with. Dr. Daniel said the reaction can release more energy than it started with, so this does not break any law. There is also enough energy to make 3 biomolecules. Example from quiz: A student is examining a chemical reaction. The student notes that the synthetic reaction requires 7.14 kcal/mol of energy per biomolecule synthesized. Also, the reaction itself produces 21.42 kcal/mol of energy. The student argues that this is enough energy to make 3 of the biomolecules. What error, if any, has the technician made in the analysis? The student has not remembered the second law of thermodynamics Cannot convert energy from one form to another at exactly 100% (7.14 kcal/mol times 3 of the biomolecules = 21.42 kcal/mol; this is exactly 100%). If the question said that the reaction needed enough energy to make 4 biomolecules instead of 3, this would violate the 1st law of thermodynamics since the student argues there is enough energy when there actually isn't.
12. In preparing a drug design, it is determined that the drug will work better if a molecule of [REDACTED] the plasma membrane of a cell. Is this plan feasible?
In preparing a drug design, it is determined that the drug will work better if a molecule of nonpolar/polar nature is anchored to the plasma membrane of a cell. In preparing a drug design, it is determined that the drug will work better if a molecule of nonpolar nature is embedded in the plasma membrane of a cell. → small nonpolar (e.g. O2 or CO2) and small uncharged polar molecules (like H2O) CAN diffuse across the membrane, but large or charged molecules require some sort of facilitated diffusion! There are channels for Na+ and Cl- ions.
33.When examining a Michaelis-Menten plot, at what point can the reaction be considered [REDACTED] order?
Is considered zero order at high substrate concentrations as the curve approaches vmax (NOT as it = Vmax since that never happens). Here, the rate of the reactant is independent of the reactant concentration. Is considered first order at low substrate concentrations. Here, the rate of the reaction depends on the concentration of one reactant. In the region between the zero-order region and the first -order region, the kinetics are mixed and difficult to interpret. Zero order: when Rate = k [A]^0 = K First order: when Rate = K1[A] Second order: when Rate = K2 [A]^2 or K2 [A] [B]
45. Alpha-ketoglutarate dehydrogenase (an enzyme) is used to test the activity of an unknown compound. Upon exposure to the compound, the enzyme is altered such that [REDACTED]. What mode of inhibition is the unknown compound exhibiting?
Look at Question 43 Example : the enzyme is altered such that all activity is nearly eliminated. The enzyme is found to have formed a covalent bond with the compound, and there is a reaction product in the solution - suicide inhibtion Example: the enzyme is altered such that all activity is nearly eliminated. However, nothing else is seen! This phenomenon occurs at femtomolar concentrations. - Transition state inhibitor
40. Calculating a Lineweaver-Burk plot reveals no change in the [REDACTED] and an increase in the [REDACTED]. What physical event could cause this?
Look at Question 43 and 41 - either competitive or noncompetitive inhibition bc no change in something No change in Vmax and an increase in Km is competitive inhibition. No change in X-intercept and an increase in Y-intercept is Noncompetitive inhibition
44. An experiment with an unknown compound on an enzyme determines the following: The [REDACTED], but [REDACTED] appears unchanged. Which of the following molecule classes is the unknown?
Look at inhibitors versus activators in Question 43 Example: The Vmax Decreases,but the Binding Appears Unchanged. Which Of The Following Molecule Classes Is The Unknown? That would be a noncompetitive inhibitor. (Page 151 in the book) The Value of Vmax decreases, but that of Km remains the same; the inhibitor does not interfere with the binding of substrate to the active site. -
37. What is one of the issues with [REDACTED] inhibition?
Look at question 43 Competitive: if there is a large amount of substrate concentration, the inhibitor cannot compete (the substrate outcompetes). Uncompetitive: need to know the enzyme substrate complex Transition state inhibitor: Irreversible and reusable How is this an issue? Noncompetitive: Many enzymes do not have allosteric sites. Suicide: Cannot be used again after it has been catalytically bound to the enzyme. Mimics the substrate. Covalently bonded.
24. Examining a mutated protein in a dangerous disease, it is determined that failure comes from a distorted alpha helix. The span of amino acids for the helix in question is found to be: [REDACTED]. What could be the cause of the distortion in the helix?
Look for proline in the sequence (creates a bend in the backbone, makes structure too rigid) 1,4 charged AA R groups (negatives or positive AA will repel each other) 1,4 "bulky" R group AAs (F, Y, W, H), this is steric hindrance Amino acid with bulky side chains are destabilizing the helix when they are 4 residues away, not when they are next to each other bc they are pointed away Anything that has glycine (it is achiral which makes it too floppy/flexible, increased entropic effects) Entropy increase Most common AAs to be in an Alpha-helix are MARKL Sample Problem: Select all that may have trouble becoming alpha helixes? KKETKSLI - has two positively charged lysine 4 away from each other KWTTKW - has two bulky tryptophan 4 away from each other and two positively charged lysine 4 away from each other HAKLPWTS - has proline, hairpin turns SWSTSWS - has big bulky Tryptophan (has rings) SQFAAGLL - has glycine LLYYAIVGSEK- increased entropy causes distortion bc the glycine is too flexible
10. Why is pH important to a biochemical system? [REDACTED]
Maintains the structure and activity of macromolecules (nucleic acids, proteins, lipids, and more). Proton dissociable groups are found in macromolecules (such as proteins) as well as the small molecules we have discussed already The cell environment is always buffered at approximately pH 7 pH changes can result in denaturation Enzymatic activity dependent on pH Experiments such as biological enzymatic assays require a certain pH In biochem system, many enzymes are tuned to specific pH environments (have ideal pH for activity)- have optimal pH. Enzymes are sensitive to change.
27. Match 5 amino acids with the correct abbreviation.
Nonpolar (hydrophobic) (uncharged): Methionine (Met, M), Tryptophan (Trp, W), Phenylalanine (Phe, F), Isoleucine (Ile, I), Leucine (Leu, L), Proline (Pro, P), Alanine (Ala, A), Valine (Val, V), Glycine (Gly, G) Polar (uncharged): Threonine (Thr, T), Cysteine (Cys, C), Tyrosine (Tyr, Y), Serine (Ser, S), Asparagine (Asn, N), Glutamine (Gln, Q) Acidic (negatively charged): Aspartic acid/aspartate (Asp, D) and Glutamic acid/Glutamate (Glu, E) Basic (positively charged): Histidine (His, H), Arginine (Arg, R), and Lysine (Lys, K) (Note: Histidine is NOT positively charged at biological pH due to side chain pKa ~6, but arginine and lysine are!)
8. Below two statements are provided, determine which (if any) are false: (i) Due to [REDACTED], ATP [REDACTED] energy upon hydrolysis; (ii) however, ATP is [REDACTED] water.
TRUE ANSWERS: First part: (i) Due to high potential energy, ATP releases energy upon hydrolysis (catabolic process) (exergonic). Energy comes from the charges on the phosphate group (not the electron density). (ii) However, ATP is stable in water (Due to charge density). 90 (not sure how 90 is related to the question, can someone please explain? It probably means that they are 90% sure about what they wrote) Due to a high negative charge density from the 3 phosphate groups, ATP releases energy upon hydrolysis; however, ATP is more stable/lower in energy in water (both true?) Second part: ATP is highly soluble in water and is quite stable in solutions between pH 6.8 and 7.4, but is rapidly hydrolysed at extreme pH. Consequently, ATP is best stored as an anhydrous salt. Below two statements are provided, determine which (if any) are false: (i) Due to the negative charge accumulation, ATP releases energy upon hydrolysis; (ii) However, ATP is expected to be unstable in water. True, false
30. What is meant by the term "spontaneous" when describing a chemical reaction?
The reaction releases energy during product formation (Answer from quiz) The energy level of the products will be less than the energy level of the reactants. Delta G<0 The reaction is exergonic *The reaction occurs on its own without the need for external energy input
31. Below two statements are provided, determine which (if any) are false: (i) Enzymes are [REDACTED] catalysts, (ii) as such they [REDACTED].
True: Enzymes are proteins that function as catalysts. Enzymes are biological catalysts Enzymes are specific. As such they: can be regulated. may be used many times for a specific purpose. Create a new reaction that has a lower activation energy. Increase the rate at which reaction reaches equilibrium. Have a greater affinity for its substrate if it has a low Km. are involved in the reaction but are not consumed. Enzymes are biological catalysts, as such they accelerate to the attainment of equilibrium False: Enzymes provide activation energy for reactions. An enzyme is least stable at the transition state (it's actually most stable here, it is the substrate that is least stable at transition state). A given enzyme will function in a laboratory the same as in the cell. Can act without binding to the substrate (it must bind). Always recognizes its substrate very quickly and easily (some have a hard time). Can achieve the potential maximum velocity (no enzyme can reach this). Alters the equilibrium point of the reaction. Reduces activation energy of a specific reaction (they rather provide an alternative pathway that has a lower activation energy)
35. Which of the following about Km is true?
True: Km is a composite of multiple steps to act as a rate constant Can be determined using the LWB equation Km is the SUBSTRATE CONCENTRATION that results in a velocity of the enzyme that is HALF of vmax The Km for a substrate will vary depending on the conditions of the reaction. Measured in M Km is analogous to binding affinity In competitive inhibition Km will increase In noncompetitive inhibition Km is unaffected In uncompetitive inhibition Km decreases Not True: All enzymes have the same Km - not true because enzymes have different vmax. The vmax depends on the amount/concentration of the enzyme and the structure of the enzyme. Since Km is the substrate concentration that results in ½ vmax, the number will be different. At the substrate concentration equal to Km, velocity of the enzyme reaction is maximal - not true because when Km = [S], velocity is ½ vmax. Km has units of concentration/seconds squared - not true because it is in M Km is ½ Vmax - Not true. Km is the CONCENTRATION at ½ Vmax At the substrate concentration equal to the Km, the enzyme is saturated with substrate - not true
39. Below two statements are provided, determine which (if any) are false: [REDACTED] phosphate groups [REDACTED], (ii) while [REDACTED] those groups.
True: Kinases add phosphate groups to serine, threonine, and tyrosine, while phosphatases remove those groups.
41. Given a Lineweaver Burk equation, what happens if [REDACTED]? (Select all that apply)
Y-intercept changes: If vmax increases, the y-intercept decreases. If vmax decreases, the y-intercept increases. X-intercept changes: If km increases, the x-intercept increases (becomes more positive/approaches zero). If km decreases, the x-intercept decreases (becomes more negative). Slope changes: If only vmax increases, the slope decreases. If vmax decreases, the slope increases. If only km increases, the slope increases. If km decreases, the slope decreases. These show the same trend as the y and x-intercepts.
13. If a system has decreasing [REDACTED] concentration, what is happening to the pH?
increasing OH concentration: the pH will increase decreasing OH concentration: the pH will decrease increasing H+ concentration: the pH will decrease (more acidic) decreasing H+ concentration: the pH will increase (more basic) pH = -log[H+] which means that pH and [H+] have a negative correlation OH and pH proportional, H and pH inversely proportional
16. What is the pH of an acetic acid solution where the concentration of acetic acid is [REDACTED] and the concentration of sodium acetate is [REDACTED]. The pKa of acetic acid is 4.76. (Use two decimal places in your answer.)
is 4.76. (Use two decimal places in your answer.) Example: acetic acid=0.3 M, sodium acetate=0.5M pH=pKa + log (A-/Ha) pH=4.76 + log (0.5/0.3) pH=4.98
28. Below two statements are provided, determine which (if any) are false: (i) At pH [REDACTED], the amino acid [REDACTED] is a zwitterion (ii) but it is [REDACTED].
more info on sheet "Below two statements are provided, determine which (if any) are false: (i) At pH 7, the amino acid S is a zwitterion (ii) but it is still charged" (NEITHER is false / BOTH ARE TRUE. Although Serine has a net charge of 0, it still has charges on the N and C terminus)
14. What is the pH of an acetic acid solution where the concentration of acetic acid is [REDACTED] and the concentration of sodium acetate is [REDACTED]. The pKa of acetic acid is 4.76. (Use two decimal places in your answer.)
pH = pKa + log ([A-]/[HA]), look at #16 for example. Example: acetic acid=0.3 M, sodium acetate=0.5M pH=pKa + log (A-/Ha) pH=4.76 + log (0.5/0.3) pH=4.98 REMEMBER TO CONVERT TO MOLAR IF NEEDED!
19. The interstellar probe Longjump-9 has been taking samples of a distant "Earth-Like'' planet. One of the samples is a previously unknown biochemical weak-acid. Given the information provided, determine the pKa of this new weak-acid. (Use two decimal places in your answer.) The pH of the world spanning ocean is [REDACTED], The concentration of the weak-acid is [REDACTED], The concentration of the conjugate base is [REDACTED].
pKa = pH - log ([A]/[HA]) HA = weak acid A= conj base Solve for PKA
29. (True / False) A researcher speculates that an enzyme has the following energy profile and that it is a reasonable profile given what we know about enzyme behavior.
question might be... (True / False) A researcher speculates that an enzyme has the following energy profile and that it is a reasonable profile given what we know about enzyme behavior: Enzyme bound to Substrate: -7.00 kcal/mol Enzyme bound to Product: -10.00 kcal/mol Enzyme in transition state: -5.00 kcal/mol It is false
32. Given the following information, determine the velocity of the system.
see image
34. Both Enzyme A & B bind a substrate with the following Michaelis-Menten constants: Enzyme A) Km = [REDACTED], Enzyme B) Km = [REDACTED], Which enzyme likely has [REDACTED]?
see image
36. Given the following information, determine the Km (in nanomolar) of the system.
see image
42. Given the following Lineweaver-Burke equation, what is the Vmax? (Remember, the Vmax is found by an intercept)
see image
43. Alpha-ketoglutarate dehydrogenase (an enzyme) is used to test the activity of an unknown compound. Upon exposure to the compound, the enzyme is altered such that [REDACTED]. What mode of inhibition is the unknown compound exhibiting?
see sheet
38. A patient suffers severe tachycardia upon consuming even a small amount of alcohol. What enzymatic issue might be the cause?
x
