MCB 450 Exam 1 Review
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Questions and Answers

Which of the following biological molecules are highly versatile?

  • Lipids
  • Nucleic acids
  • Water
  • Carbohydrates
  • Proteins (correct)

Which of the following enzyme is responsible for the formation of peptide bonds in proteins?

  • DNA or RNA polymerase
  • glycogen synthase
  • peptidyltransferase (correct)
  • acyltransferase
  • Lipase

Hydrogen bonds mostly occur between hydrogen and which other atoms?

  • Oxygen and nitrogen (correct)
  • Silicon and Germanium
  • Sodium and magnesium
  • Neon, argon, and xenon
  • Scandium and vanadium

Which of the following is an amphipathic molecule?

<p>Bile acid (E)</p> Signup and view all the answers

Which of the following is necessarily characterized by a non-covalent linkage?

<p>Ionic bond (B)</p> Signup and view all the answers

Which of the following processes is powered by a hydrophobic interaction?

<p>Membrane formation (E)</p> Signup and view all the answers

What is the concentration of a NaOH solution with a pH of 12.7?

<p>0.05 M (E)</p> Signup and view all the answers

The pH of a buffered solution is 4.97. What is the approximate ratio of the concentration of acid to conjugate base if the pKa of the acid is 3.97?

<p>10:1 (C)</p> Signup and view all the answers

What accounts for peptide bond planarity within a polypeptide?

<p>Partial double bond character of the peptide bond. (D)</p> Signup and view all the answers

Which of the following are hydrophobic molecules?

<p>Nonpolar molecules (A)</p> Signup and view all the answers

Proline is called “alpha-helix breaker” because of its

<p>nitrogen atom in the peptide linkage has no hydrogen atom to participate in hydrogen bonds with other amino acids. (B)</p> Signup and view all the answers

Which of the following interactions contributes to the secondary structure of a protein?

<p>Hydrogen bonds between amino groups and carbonyl groups of different amino acids. (E)</p> Signup and view all the answers

__________ structure involves interactions between the various side chains of amino acids.

<p>Tertiary (C)</p> Signup and view all the answers

Which of the following type of bonds is involved in the tertiary structure of protein folding?

<p>Disulfide bond (C)</p> Signup and view all the answers

When cooking an egg, opening the egg over a hot pan causes the non-yolk part of the egg to go from clear and viscous to white and solid. Adding heat to the egg white protein part of the egg is part of a process called what?

<p>Denaturation (A)</p> Signup and view all the answers

Which of the following is a protein-misfolding disease?

<p>Alzheimer's disease (AD) (E)</p> Signup and view all the answers

Listed below are some zymogens together with their putative activators. Select the pair that is incorrectly matched.

<p>Pepsinogen---activated by trypsin (D)</p> Signup and view all the answers

Hartnup disease results from the genetic defect in the transporter gene, SLC6A19, which is responsible for the absorption of which of the following amino acids?

<p>Tryptophan (B)</p> Signup and view all the answers

Which of the following glycosidic bonds cannot be broken down by human digestive enzymes?

<p>β-1,4 Glycosidic bond in cellulose (B)</p> Signup and view all the answers

Lactose intolerance is due to the deficiency of which of the following enzymes?

<p>lactase (C)</p> Signup and view all the answers

Which of the following statements is NOT true regarding lipid digestion?

<p>Lipid can only be digested in stomach and small intestine. (A)</p> Signup and view all the answers

What is the major role of bile salts in lipid metabolism?

<p>They break up (emulsify) the fat globules into smaller hydrophilic coated droplets. (B)</p> Signup and view all the answers

Which of the following is NOT true regarding micelles in the intestine?

<p>They are transport vehicles after triglycerides and proteins bind during lipid digestion. (A)</p> Signup and view all the answers

What is the function of ApoCII in mature chylomicrons?

<p>It is necessary for the activation of lipoprotein lipase in some tissues. (A)</p> Signup and view all the answers

Steatorrhea is the presence of excess fat in feces due to poor digestion and malabsorption. Which of the following defect or deficiency in a disorder is likely associated with steatorrhea?

<p>Lack of bile acids (C)</p> Signup and view all the answers

ALT (Alanine aminotransferase) and AST (aspartate aminotransferase) are abundant in liver and can be used as plasma markers for liver diseases. What is the major function of these enzymes in liver?

<p>Transfer the amino groups of different amino acids to a-ketoglutarate. (D)</p> Signup and view all the answers

Amino groups of amino acids can be used for the synthesis of other nitrogen-containing molecules. What is the source of the two nitrogens in urea? I. Glutamate II. Alanine III. Aspartate IV. NH3

<p>III, IV (C)</p> Signup and view all the answers

A deficiency in which of the following enzymes would directly limit the ability of the body to fix and dispose of ammonia?

<p>Carbamoyl phosphate synthetase I (CPS-I) (B)</p> Signup and view all the answers

Which of the following statements is TRUE for the disposal of nitrogen in hibernating bears?

<p>Urea from liver is transported to small intestine to be converted to NH4+ for reuse in amino acid synthesis. (B)</p> Signup and view all the answers

A patient with PKU (Phenylketonuria) should be put on a life-long diet restricting which of the following?

<p>Phenylalanine (E)</p> Signup and view all the answers

Which of the following co-factor is involved in the synthesis of succinyl CoA from L-methylmalonyl CoA?

<p>Deoxyadenosylcobalamin (D)</p> Signup and view all the answers

Which of the following reactions is an example of ammonia fixation?

<p>Alpha-ketoglutarate is converted to glutamate by glutamate dehydrogenase. (A)</p> Signup and view all the answers

What enzyme is deficient in Maple Syrup Urine Disease (MSUD)?

<p>branch-chain alpha-keto acid dehydrogenase (A)</p> Signup and view all the answers

Which of the following answers completes the sentence correctly? Guanosine is a

<p>purine nucleoside. (B)</p> Signup and view all the answers

Mycophenolic acid is a drug used to prevent graft rejection by inhibiting an enzyme in de novo purine synthesis. What is the direct target of this drug?

<p>IMP dehydrogenase (C)</p> Signup and view all the answers

Lesch-Nyhan syndrome is caused by

<p>mutations in the HGPRT (Hypoxanthine-guanine phosphoribosyltransferase) gene. (E)</p> Signup and view all the answers

Degradation of which of the following products leads to the production of uric acid during the digestive process?

<p>Purines (D)</p> Signup and view all the answers

What is the carbon source for the carbamoyl phosphate in pyrimidine synthesis?

<p>CO2 (D)</p> Signup and view all the answers

What is the direct target of 5-Fluorouracil, a drug widely used in chemotherapy in cancer?

<p>Thymidylate synthase (C)</p> Signup and view all the answers

Urine FIGlu test could be an indicator of the deficiency of which of the following vitamin?

<p>Vitamin B12 (A)</p> Signup and view all the answers

Human dihydrofolate reductase can be effectively and specifically inhibited by the administration of:

<p>methotrexate (A)</p> Signup and view all the answers

N5, N10-methylene-THF is the first THF (tetrahydrofolate) derivative generated in cells in one carbon metabolism. Which of the following amino acid provides this methylene (-CH2-) group?

<p>Serine (A)</p> Signup and view all the answers

What is the source of electrons entering complex II?

<p>FADH2 from the TCA cycle (B)</p> Signup and view all the answers

In the electron transport chain, what are the pair of electron carriers in and out of complex III?

<p>QH2→cytochrome C (D)</p> Signup and view all the answers

There are 3 conformations of the beta subunit of ATP synthase, with each representing different state of this enzyme. Which conformation represents the active state of ATP synthase for the synthesis of ATP?

<p>T (tight) form (C)</p> Signup and view all the answers

Many of the carriers in the electron transport chain are cytochromes. The central component of the cytochrome capable of redox reactions is

<p>an iron atom (E)</p> Signup and view all the answers

Why is oxygen necessary in aerobic cellular respiration?

<p>It is the final electron acceptor in the electron transport chain. (C)</p> Signup and view all the answers

Flashcards

Proteins

Versatile biological molecules that perform a vast array of functions in the cell, including catalysis, transport, and structure.

Peptidyltransferase

Enzyme responsible for catalyzing the formation of peptide bonds between amino acids during protein synthesis.

Hydrogen bond

A weak type of non-covalent bond that commonly occurs between a hydrogen atom and either an oxygen or nitrogen atom

Amphipathic molecule

A molecule that has both hydrophobic and hydrophilic regions, allowing it to interact with both polar and nonpolar environments.

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Non-covalent linkage

A linkage formed by weak electrostatic forces.

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Hydrophobic interaction

Interaction that drives the association of nonpolar molecules/regions in an aqueous environment to minimize contact with water.

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Denaturation

The unfolding and disorganization of a protein's native structure due to the disruption of non-covalent interactions.

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Protein-misfolding disease

Diseases caused by the accumulation of misfolded proteins, which can form aggregates and disrupt cellular function.

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Zymogen

Inactive precursor of an enzyme that requires a biochemical change (such as hydrolysis) to become an active enzyme.

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Hartnup disease

A genetic disorder affecting the absorption of tryptophan and other neutral amino acids.

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β-1,4-Glycosidic bond

A type of glycosidic bond that cannot be broken down by human digestive enzymes.

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Lactose Intolerance

A condition caused by a deficiency of lactase, the enzyme that breaks down lactose.

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Bile salts

Emulsify fats into smaller droplets.

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Micelles

Water-soluble microdroplets that transport digested lipids to the intestinal cells for absorption.

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ApoCII

Activates lipoprotein lipase.

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Steatorrhea

The presence of excess fat in feces due to poor digestion and malabsorption

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ALT/AST function

Transfer amino groups to α-ketoglutarate.

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Nitrogen source in urea

Aspartate and NH3.

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CPS-I

Enzyme whose deficiency would limit the bodies ability to fix and dispose ammonia.

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PKU diet

A diet restricting phenylalanine.

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Deoxyadenosylcobalamin

Used in synthesis of succinyl CoA from L-methylmalonyl CoA

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Ammonia fixation

Alpha-ketoglutarate converted to glutamate.

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MSUD deficient enzyme

Branch-chain alpha-keto acid dehydrogenase.

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Guanosine

A purine nucleoside.

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Mycophenolic acid's target

Inhibits IMP dehydrogenase, involved in the synthesis of guanine nucleotides.

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Lesch-Nyhan cause

Mutations in the HGPRT gene.

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Uric acid

Purines

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Carbamoyl phosphate carbon source

CO2

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5-Fluorouracil target

Thymidylate synthase

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Urine FIGlu indicator

Vitamin B12

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Study Notes

  • Exam 1 for MCB 450 was held on February 8, 2024.

  • The exam consisted of 50 questions, totaling 150 points.

  • Proteins are highly versatile biological molecules.

  • Peptidyltransferase is responsible for the formation of peptide bonds in proteins.

  • Hydrogen bonds mostly occur between hydrogen, oxygen, and nitrogen atoms.

  • Bile acid is an example of an amphipathic molecule.

  • Ionic bonds are characterized by non-covalent linkages.

  • Membrane formation is powered by hydrophobic interactions.

  • A NaOH solution with a pH of 12.7 has a concentration of 0.05 M.

  • For a buffered solution with a pH of 4.97 and an acid pKa of 3.97, the approximate ratio of acid to conjugate base is 1:10.

  • Peptide bond planarity within a polypeptide is accounted for by the partial double bond character of the peptide bond.

  • Nonpolar molecules are hydrophobic.

  • Proline is called an "alpha-helix breaker" because the nitrogen atom in the peptide linkage has no hydrogen atom to participate in hydrogen bonds with other amino acids.

  • Hydrogen bonds between amino groups and carbonyl groups of different amino acids contribute to the secondary structure of a protein.

  • Tertiary structure involves interactions between the various side chains of amino acids.

  • Disulfide bonds are involved in the tertiary structure of protein folding.

  • Denaturation is the process where the non-yolk part of an egg goes from clear and viscous to white and solid when cooked.

  • Alzheimer's disease (AD) is a protein-misfolding disease.

  • Pepsinogen activated by trypsin is an incorrectly matched zymogen/activator pair.

  • Hartnup disease results from a genetic defect in the transporter gene, SLC6A19, affecting tryptophan absorption.

  • α-1,4-Glycosidic bonds cannot be broken down by human digestive enzymes.

  • Lactose intolerance is due to a deficiency in lactase.

  • "Lipid can only be digested in the stomach and small intestine" is NOT true regarding lipid digestion i.e lipid digestion actually starts in the mouth by lingual lipase.

  • Bile salts break up (emulsify) fat globules into smaller hydrophilic coated droplets, playing a major role in lipid metabolism.

  • Micelles are NOT transport vehicles after triglycerides and proteins bind during lipid digestion.

  • ApoCII in mature chylomicrons is necessary for the activation of lipoprotein lipase in some tissues.

  • Steatorrhea is likely associated with a lack of bile acids.

  • ALT and AST in the liver transfer the amino groups of different amino acids to α-ketoglutarate.

  • Aspartate and NH3 are the source of the two nitrogens in urea.

  • A deficiency in carbamoyl phosphate synthetase I (CPS-I) would directly limit the ability of the body to fix and dispose of ammonia.

  • Urea from the liver is transported to the small intestine to be converted to NH4+ for reuse in amino acid synthesis in hibernating bears.

  • A patient with PKU (Phenylketonuria) should restrict phenylalanine on a life-long diet.

  • Deoxyadenosylcobalamin is a co-factor involved in the synthesis of succinyl CoA from L-methylmalonyl CoA.

  • Alpha-ketoglutarate being converted to glutamate by glutamate dehydrogenase is an example of ammonia fixation.

  • The deficient enzyme in Maple Syrup Urine Disease (MSUD) is branch-chain alpha-keto acid dehydrogenase.

  • Guanosine is a purine nucleoside.

  • Mycophenolic acid prevents graft rejection by inhibiting IMP dehydrogenase.

  • Lesch-Nyhan syndrome is caused by mutations in the HGPRT (Hypoxanthine-guanine phosphoribosyltransferase) gene.

  • Degradation of purines leads to the production of uric acid during the digestive process.

  • The carbon source for carbamoyl phosphate in pyrimidine synthesis is CO2.

  • Thymidylate synthase is the direct target of 5-Fluorouracil, a widely used drug in chemotherapy for cancer.

  • A Urine FIGlu test is conducted to detect a deficiency in Vitamin B12.

  • Human dihydrofolate reductase can be effectively and specifically inhibited by the administration of methotrexate.

  • Serine provides the methylene (-CH2-) group for N5, N10-methylene-THF in one carbon metabolism.

  • FADH2 from the TCA cycle is the source of electrons entering complex II.

  • QH2→cytochrome C are the pair of electron carriers in and out of complex III in the electron transport chain.

  • The T (tight) form represents the active state of ATP synthase for the synthesis of ATP.

  • The central component of the cytochrome capable of redox reactions is an iron atom.

  • Oxygen serves as the final electron acceptor in the electron transport chain.

  • Dicyclohexylcarbodiimide (DCC) inhibits ATP synthase by binding to the carboxylate group of glutamate of the C subunit.

  • Electron transfer from the cytosol to the matrix if using the glycerol 3-phosphate shuttle may yield less ATP than mitochondrial NADH.

  • 2,4-dinitrophenol (DNP) prevents ATP synthesis while allowing electron transport to proceed because DNP can transport protons across the membrane, dissipating the proton gradient.

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Review of Exam 1 for MCB 450 held on February 8, 2024, covering proteins, peptide bonds, hydrogen bonds, and amphipathic molecules. Focus on ionic bonds, hydrophobic interactions, pH calculations, and peptide bond characteristics. Also covers proline's role as an alpha-helix breaker.

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