Biochemistry Module 1 Quiz
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Questions and Answers

Which of the following is NOT a type of protein structure?

  • Tertiary
  • Quaternary (correct)
  • Secondary
  • Primary
  • Which of the following amino acid modifications is NOT commonly found in proteins?

  • Phosphorylation
  • Hydrogenation (correct)
  • Methylation
  • Glycosylation
  • Which of the following is a key characteristic of a transmissible spongiform encephalopathy (TSE)?

  • Treatable with antibiotics
  • Prions cause misfolding of proteins (correct)
  • High fever and flu-like symptoms
  • Caused by a virus
  • What is the name of the process that removes a water molecule during the formation of a peptide bond?

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

    Which type of inhibitor binds to the enzyme active site and prevents the substrate from binding?

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

    Which of the following is NOT a characteristic of a lipid?

    <p>Acts as a primary energy source for cells (B)</p> Signup and view all the answers

    Which of the following is a type of transmembrane protein involved in neurotransmitter release?

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

    What type of transport does NOT require energy to move molecules across the cell membrane?

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

    Signup and view all the answers

    Study Notes

    Module 1 Material

    • Chapter 1: Covers hydrolysis, compartmentation, natural selection, evolution, cell sizes, cell components, and the differences between viruses, prokaryotes, eukaryotes, and archaea, including thermodynamics and units.

    Module 1 Material - Chapter 2

    • Chapter 2: Focuses on the hydrophobic effect, osmosis, water structure/properties, and bonding types (hydrogen, London dispersion, hydrophobic, ionic). Key concepts include pKa, pH values, amphiphiles, and ion mobility, along with Kw values.

    Module 1 Material - Chapter 3

    • Chapter 3: Details amino acids (structure, groupings, pKas, modifications), protein structure, amino acid pairings, chirality, zwitterions, peptide formation, and drugs.

    Module 1 Material - Chapter 4

    • Chapter 4: Explores protein structure (alpha-helices, beta-sheets, beta-strands, beta-hairpins, disulfides, folding), oligomeric and globular proteins, collagen, Alzheimer's plaques, transmissible spongiform encephalopathies, prions, and 3D protein structural determination.

    Module 2 Material - Chapter 9

    • Chapter 9: Covers catalysis, enzyme-substrate interactions, lysozymes, serine protease (steps and tetrahedral intermediates), RNase, enzyme classification, delta-G, transition states, nucleophilicity, and metalloenzymes.

    Module 2 Material - Chapter 10

    • Chapter 10: Focuses on Michaelis-Menten kinetics (Km, Kcat, Vmax, Vo, etc.), inhibitors (types, plots, Ki), noncovalent modifications, and regulation in enzyme reactions, including reaction orders, rate of elementary reactions, steady-state kinetics, and ATCase's T and R states.

    Module 3 Material - Chapter 5

    • Chapter 5: Outlines sugar structures (structures, isomers, polymers), amylopectin, amylose, hyaluronic acid, cellulose, chitin, peptidoglycans, glycosylation, hemiacetals, uronic acid, sialic acid, and peptidoglycans, as well as artificial sweeteners.

    Module 3 Material - Chapter 7

    • Chapter 7: Discusses lipids (structures, locations, properties), cholesterol, and lipid bilayers.

    Module 3 Material - Chapter 8

    • Chapter 8: Covers transmembrane proteins, micelles, adipocytes, biconcave structure, fluid-mosaic models, translocons, vitamin D, SNAREs, I-cells, Botox, clathrin, endocytosis, and palmitolyation. It also details transporter types, uses, differences, common molecules that can pass through (neurotransmitters, gap junctions, diffusion, and aquaporins).

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    CHE 330 Exam 1 Study Guide PDF

    Description

    Test your knowledge on the fundamental concepts of biochemistry covered in Module 1. This quiz encompasses topics from various chapters including hydrolysis, protein structure, and hydrophobic effects. Prepare to dive deep into cellular components, thermodynamics, and amino acid properties.

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