Cell and Molecular Biology Introduction
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Which of the following correctly describes the relationship between the equilibrium constant (Keq) and the direction of an enzymatic reaction?

  • A low Keq indicates that the reaction favors the formation of products.
  • A high Keq indicates that the reaction favors the formation of reactants.
  • A high Keq indicates that the reaction favors the formation of products. (correct)
  • Keq does not influence the direction of the reaction.
  • What is the difference between competitive and noncompetitive inhibitors?

  • Competitive inhibitors are irreversible, while noncompetitive inhibitors are reversible.
  • Competitive inhibitors increase the enzyme's activity, while noncompetitive inhibitors decrease the enzyme's activity.
  • Competitive inhibitors bind to the active site, preventing substrate binding, while noncompetitive inhibitors bind to a different site, altering the enzyme's shape and reducing its activity. (correct)
  • Competitive inhibitors bind to a different site, altering the enzyme's shape and reducing its activity, while noncompetitive inhibitors bind to the active site, preventing substrate binding.
  • Which of the following correctly describes the relationship between KM and the affinity of an enzyme for its substrate?

  • A low KM indicates a low affinity, meaning the enzyme binds its substrate loosely.
  • KM does not reflect the affinity of an enzyme for its substrate.
  • A high KM indicates a low affinity, meaning the enzyme binds its substrate loosely. (correct)
  • A high KM indicates a high affinity, meaning the enzyme binds its substrate tightly.
  • Which of the following is an example of an Hsp70 chaperone?

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

    Which of the following correctly describes the difference between PrPc and PrPsc?

    <p>PrPc is a normal cellular protein, while PrPsc is a misfolded form that aggregates and causes disease. (C)</p> Signup and view all the answers

    Which level of protein structure is primarily determined by hydrogen bonding between the backbone atoms of the polypeptide chain?

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

    Which of the following describes the process of a thermodynamically unfavorable reaction occurring in a cell?

    <p>The reaction is coupled to a thermodynamically favorable reaction, providing energy to drive the unfavorable reaction. (A)</p> Signup and view all the answers

    Which of the following correctly describes the structure of a carboxyl group below its pK?

    <p>It exists as a carboxylate ion (COO-) with a negative charge. (D)</p> Signup and view all the answers

    What is the main source of trans fats in the diet?

    <p>Partially hydrogenated vegetable oils (D)</p> Signup and view all the answers

    Which of the following statements about the structure of α-helices and β-pleated sheets is TRUE?

    <p>Both α-helices and β-pleated sheets are formed by hydrogen bonding between backbone atoms. (A)</p> Signup and view all the answers

    What is the primary function of the Golgi apparatus in a eukaryotic cell?

    <p>Modification and packaging of proteins (A)</p> Signup and view all the answers

    Which of the following covalent bonds is considered polar due to the difference in electronegativity between the atoms involved?

    <p>O-H (B)</p> Signup and view all the answers

    Which of the following functional groups is NOT capable of forming hydrogen bonds?

    <p>Methyl (-CH3) (C)</p> Signup and view all the answers

    What is the key structural difference that distinguishes starch from cellulose, both being polymers of glucose?

    <p>Starch contains only alpha-glucose, while cellulose contains only beta-glucose. (D)</p> Signup and view all the answers

    Which of the following statements accurately describes the properties of life that are also shared by cells?

    <p>Cells exhibit growth, reproduction, and response to stimuli. (B)</p> Signup and view all the answers

    The endosymbiotic theory states that:

    <p>Mitochondria and chloroplasts originated from free-living bacteria. (A)</p> Signup and view all the answers

    In the context of cell theory, what is the primary function of the nucleus?

    <p>Storage and protection of genetic material (DNA). (D)</p> Signup and view all the answers

    Which of the following is NOT considered a basic property of cells?

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

    Which of the following is NOT common to both eukaryotes and prokaryotes?

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

    Different laboratory methods allow scientists to isolate specific cellular organelles, so that they can study some cellular processes in more detail. Which organelle would you try to isolate if you wanted to study the enzymes involved in lipid synthesis?

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

    According to the theory of endosymbiosis promoted by ______, our earliest prokaryotic ancestor was an ______, who ingested an ______, the precursor of modern day mitochondria. Ingestion of a second endosymbiont, a ______, later evolved into chloroplasts.

    <p>Lynn Margulis; anaerobic heterotroph; aerobic prokaryote; cyanobacteria</p> Signup and view all the answers

    Which of the following is NOT a property of covalent and non-covalent bonds?

    <p>Non-covalent bonds require a large amount of energy to break (A)</p> Signup and view all the answers

    Based on the following table of electronegativity, which of the following represents the order of polarity, most to least?

    <p>O – H = C=O C=O = C-H O=O = O—H C-S = O-H</p> Signup and view all the answers

    In a covalent bond formed between Nitrogen and a less electronegative atom, the N atom would have a ______ while the less electronegative atom would have a ______ charge.

    <p>partial negative; partial positive</p> Signup and view all the answers

    Particular groupings of atoms that often behave as a unit and give organic molecules their physical properties, chemical reactivity and solubility in aqueous solutions are known as:

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

    Which of the following characteristics below (from 1 to 7) are typical of the polysaccharide cellulose?

    <p>1, 3, 4, 5, 7 (B)</p> Signup and view all the answers

    Compounds rich in [blank] tend to be liquid at room temperature. These compounds can be altered so they are solid at room temperature by [blank].

    <p>unsaturated fats = Increasing the amount of double bonds saturated fats = Decreasing the amount of single bonds</p> Signup and view all the answers

    The following structures represent ______, which are maintained ______ at room temperature, due to the ______ of double bonds.

    <p>saturated fats; solid; absence</p> Signup and view all the answers

    A patient with hyperlipidemia has been counseled to reduce the saturated fats in his diet, so he has replaced butter with a butter substitute that he knows is made from a polyunsaturated oil. The manufacturer of this butter substitute has partially hydrogenated this product. Which one of the following is the best description of why this product was partially hydrogenated?

    <p>Hydrogenation reduces the double bonds, creating a more saturated product, which is more marketable. (D)</p> Signup and view all the answers

    As a scientist you find an unknown sample and run some tests to identify this unknown sample. Molecular analysis found glycerol, fatty acids, phosphate and choline. Given this, which conclusion is most probable?

    <p>It is only phospholipid. (D)</p> Signup and view all the answers

    You treat a partially purified preparation of protein with mercaptoethanol, a reagent that can break bonds formed between sulfur atoms. Which level of protein structure is likely to be affected?

    <p>C and D are correct (E)</p> Signup and view all the answers

    Amino acids 1 to 4 are all part of the same solution at a particular pH. If kept at the same pH, hydrogen bonds, could be formed between the R groups of: (See figures in document)

    <p>Between 1 and 3 (D)</p> Signup and view all the answers

    Amino acids 1 to 4 are all part of the same solution at a particular pH. If kept at the same pH, ionic bonds could be formed between the R groups of: (See figures in document)

    <p>None of these pairs is capable of forming ionic bonds unless pH is changed (D)</p> Signup and view all the answers

    How many amino acids are in this peptide?: (See figure in document)

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

    What is the role of misfolded proteins in Creutzfeld-Jakob Disease?

    <p>B, C and D are correct. (C)</p> Signup and view all the answers

    Free energy is ______. A reaction will be spontaneous when ______

    <p>the energy available to do work; the free energy of the reactants is lower than that of the products</p> Signup and view all the answers

    Conversion of A → B is an endergonic reaction. Which of the following reactions could be coupled with A→B so that both A→B and C D can occur?

    <p>Both A and C (D)</p> Signup and view all the answers

    The continual flow of oxygen and other materials into and out of cells allows cellular metabolism to exist in a steady state because

    <p>The concentrations of reactants and products remain relatively constant. (C)</p> Signup and view all the answers

    Enzymes speed up reactions by lowering the ______. This can be accomplished by forming an enzyme-substrate complex, where the R chains of the amino acids in the enzyme's ______ and the substrate are bound together by ______.

    <p>activation energy; active site; noncovalent bonds</p> Signup and view all the answers

    Dissolving a sugar cube in water and breaking down complex glycogen molecules into smaller molecules are examples of decrease in entropy in a system.

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

    The amino acids glutamine and glutamic acid are shown below. They differ only in the structure of their side chains (circled). At pH 7, glutamic acid can participate in molecular interactions that are not possible for glutamine. What types of interactions are these? (See figure in the document)

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

    Which of the following amino acids has side chains with the greatest potential to form a) hydrogen-bonds b) ionic-bonds and c) hydrophobic interactions? (assume you don't change the pH) (See figure in the document)

    <p>a) 4; b) 2; c) 1 = a) 3; b) 1; c) 5</p> Signup and view all the answers

    You mix reagents (A, B, C, D) so that each is present at an initial concentration of

    <p>[0.25][0.25] / [0.15] [0.15] (E)</p> Signup and view all the answers

    What type of bond is this and what structure do long chains of this make up? (See figure in the document)

    <p>Beta1,4 Cellulose (B)</p> Signup and view all the answers

    A fatty acid consists of three hydrocarbon chains linked to a glycerol backbone.

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

    Is the following statement correct? “Amino acids used in making a polypeptide have an amino group and a carboxyl group, and these groups can be present on any carbon atoms”

    <p>No, amino acids require a very specific structure and must have all groups attached to the alpha carbon. (A)</p> Signup and view all the answers

    An enzyme in the liver that removes glucose from blood has a high K™; another that does the same thing in brain tissue has a small K™. Which of the following options would BEST describe how this information would relate to glucose uptake in an organism?

    <p>The enzyme in brain tissue can take glucose from the bloodstream even when levels are low, and the enzyme in liver will not take glucose from blood unless levels are high (C)</p> Signup and view all the answers

    Flashcards

    Cell Theory

    Three fundamental principles about cells: all living things are made of cells, cells are the basic unit of life, and all cells arise from pre-existing cells.

    Lynn Margulis

    A prominent biologist known for her theory on the symbiotic origin of eukaryotic cells.

    Electronegativity

    A measure of an atom's ability to attract and hold electrons, varying across the periodic table.

    Polar Covalent Bonds

    Chemical bonds where electrons are shared unequally, resulting in a molecule with a partial positive and negative charge.

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    Acids and Bases

    Acids increase H+ concentrations in solution, while bases increase OH- concentrations, both affecting pH.

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    Types of Noncovalent Bonds

    Weak chemical bonds, including ionic, hydrogen, and Van der Waals forces, essential for molecular interactions.

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    Cell Structures

    Key components include membranes, walls, nucleus, and organelles, each with specific functions.

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    Functional Groups

    Specific groups of atoms within molecules that determine the molecule's chemical reactivity and properties.

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    Saturated Fatty Acid

    A fatty acid with no double bonds between carbon atoms; typically solid at room temperature.

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    Unsaturated Fatty Acid

    A fatty acid that contains one or more double bonds; usually liquid at room temperature.

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    Trans Fats

    Unsaturated fats that have been hydrogenated, often found in processed foods.

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    pKa

    The negative logarithm of the acid dissociation constant; indicates the strength of an acid.

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    Endergonic Reaction

    A reaction that absorbs energy, leading to a positive ΔG value.

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    Exergonic Reaction

    A reaction that releases energy, leading to a negative ΔG value.

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    Equilibrium Constant (Keq)

    A constant that expresses the ratio of product and reactant concentrations at equilibrium.

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    Enzyme

    A protein that acts as a catalyst to accelerate a chemical reaction.

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    Native Protein Structure

    The functional three-dimensional structure of a protein in its active form.

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    Chaperone Proteins

    Proteins that assist in the folding and stabilization of other proteins.

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    Eukaryotes vs Prokaryotes

    Eukaryotes have a nucleus; prokaryotes do not.

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    Lipid Synthesis Organelle

    The endoplasmic reticulum is crucial for lipid synthesis.

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    Endosymbiosis Theory

    Lynn Margulis proposed that eukaryotic cells arose from prokaryotes.

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    Covalent Bonds

    Bonds formed by shared electrons between atoms.

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    Non-Covalent Bonds

    Weak interactions like hydrogen bonds and ionic bonds.

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    Polarity Order

    Polarity of bonds is affected by electronegativity.

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    Charge in Covalent Bonds

    In a bond with N and a less electronegative atom, N is partially positive.

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    Cellulose Properties

    Cellulose consists of β(1→4) linked glucose polymers.

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    Unsaturated Fats

    Fats that are liquid at room temperature.

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    Hydrogenation Effect

    Partially hydrogenated oils become more saturated.

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    Protein Structure

    Mercaptoethanol affects tertiary and quaternary structures.

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    Misfolded Proteins Role

    Misfolded proteins propagate their structure and can be infectious.

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    Free Energy

    Energy available to do work in a system.

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    Endergonic and Coupled Reactions

    Endergonic reactions can couple with exergonic for energy.

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    Cell Metabolism Steady State

    The constant flow of materials maintains cellular functions.

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    Enzyme Function

    Enzymes speed up reactions by lowering activation energy.

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    Entropy Change

    Dissolving sugar in water increases system entropy.

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    Amino Acid Interactions

    Different R groups allow for unique interactions in proteins.

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    Peptide Length

    Count of amino acids in a polypeptide.

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    Ionic Bonds in Amino Acids

    Ionic interactions occur between charged R groups.

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    Sugar and Glycerol

    Glycerol does not link three hydrocarbon chains in fats.

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    Amino Acid Structure

    Amino acids must have both an amino and carboxyl group on the alpha carbon.

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    KM Values

    A high KM indicates an enzyme needs high substrate concentration.

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    Glycogen Breakdown

    Breaking down glycogen decreases entropy at first.

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    Study Notes

    Cell and Molecular Biology Introduction

    • Prokaryotic, Plant, and Animal Cell Diagrams: Students should draw and label diagrams of prokaryotic, plant, and animal cells, emphasizing the functions of components like cell membrane, cell wall, nucleus, genetic material, ribosomes, rough ER, smooth ER, Golgi, mitochondria, chloroplast, lysosome, peroxisome, vacuole, microtubules, actin filaments, and intermediate filaments.

    • Cell Theory Tenets: Students must list and explain the three tenets of Cell Theory.

    • Five Cell Properties: Detail five fundamental properties of cells, distinguishing them from the fundamental properties of life.

    • Lynn Margulis's Contribution: Describe Lynn Margulis and her key contribution to cellular biology, focusing on her symbiotic theory, and how it explains the origin of mitochondria and chloroplasts.

    • Mitochondrial and Chloroplast Origin: Outline the evidence supporting the endosymbiotic theory, particularly for the origins of mitochondria and chloroplasts in modern eukaryotes. Include examples of evidence such as double membranes and their own DNA. Describe prokaryotic ancestor ingesting aerobic prokaryote to form mitochondrial ancestor and another ingestion event forming chloroplast ancestor from cyanobacteria.

    Basic Chemistry

    • Electronegativity Trends: Define electronegativity, explaining how it changes across the periodic table. Electronegativity is the tendency of an atom to attract shared electrons in a covalent bond.

    • Polar vs. Nonpolar Covalent Bonds: Determine whether covalent bonds (HCl, CO2, CH4, H2O, H2S, NH3) are polar or nonpolar based on electronegativity differences.

    • Noncovalent Bond Types: Describe the properties and characteristics of distinct types of noncovalent bonds (hydrogen bonds, ionic bonds, van der Waals interactions).

    • Functional Groups and Hydrogen Bonding: Draw and identify functional groups on a table, specifying which can form hydrogen bonds. Note which bond types (hydrogen, ionic, van der Waals) are important to protein folding and function.

    • Acids and Bases: Define acids and bases, and explain the influence of acids and bases on pH through impacting H+ and OH- concentrations in aqueous solutions. Give examples of each in water.

    Carbohydrates, Lipids, and Proteins

    • Polymer Structures: Draw and label glycogen, starch, and cellulose molecules, each with at least six glucose monomers. Identify the bonds responsible for their structure, noting examples of where each polymer is found.
    • Lipid Structures: Draw the general structures of fatty acids, fats, and phospholipids. Identify and label functional groups in these structures using the table.
    • Saturated vs. Unsaturated Fatty Acids: Define saturated and unsaturated fatty acids, highlighting structural differences and melting temperatures. Define trans fats and their primary sources (note industrial hydrogenation process).
    • pK Values and Functional Groups: Define pK (pKa) and illustrate the structures of a carboxyl group and an amino group above and below their respective pKs. Note how pK values relate to pH and ionization states of these groups in proteins.

    Thermodynamics and Free Energy

    • Thermodynamic Definitions: Define key terms like internal energy (E), exothermic, endothermic, spontaneous, thermodynamically favorable, entropy, free energy (ΔG), exergonic, and endergonic.

    • Laws of Thermodynamics: Describe the two laws of thermodynamics and the concept of "events in the universe tending to go downhill" with an example.

    • Endergonic Reactions in Cells: Explain how endergonic reactions occur in cells despite being thermodynamically unfavorable through coupling with exergonic reactions (a very important point).

    • Equilibrium Constant (Keq): Define equilibrium constant (Keq) and explain its relationship to the direction of an enzymatic reaction. Note how Keq values relate to the relative concentrations of products and reactants at equilibrium.

    • Equilibrium vs. Steady State Metabolism: Compare and contrast equilibrium and steady-state metabolism, analyzing how open systems are maintained far from equilibrium.

    Enzymes I

    • Enzyme Definitions: Define enzyme, coenzyme, cofactor, turnover number, activation energy, activation energy barrier, transition state, and active site.

    • Enzymatic Reaction Diagram: Label and explain a diagram depicting the free energy changes in a reaction with and without an enzyme, emphasizing transition state, activation energy, and substrates/products.

    Higher Order of Protein Structure

    • pK Values and Functional Groups: Define pK (pKa) and illustrate the structures of a carboxyl group and an amino group above and below their respective pKs.

    • Amino Acid Classification: Classify amino acids as polar charged, polar uncharged, or nonpolar based on R-group properties (refer to Figure 2.28).

    • Protein Structure Levels: List and describe the four levels of protein structure and the types of bonds responsible for each.

    • Secondary Structure (α-helix and β-sheet): Compare and contrast α-helices and β-pleated sheets, illustrating the hydrogen bonding patterns. Add that secondary structures are stabilized by hydrogen bonds.

    • Tertiary and Quaternary Structure Bonds: Identify and illustrate how side chains of different amino acids form noncovalent bonds to create tertiary and quaternary structures (refer to Figure 2.38). Include details about ionic interactions, hydrogen bonds, hydrophobic interactions, and disulfide bonds.

    Protein Conformation and Chaperones

    • Protein Folding Definitions: Define protein unfolding, protein folding, and native structure.

    • Chaperone Function: Describe the purpose and importance of chaperones, explaining how they bind to nascent proteins (refer to Figure 2.48). Explain that chaperones assist in proper protein folding and prevent aggregation.

    • PrP C and PrP Sc Comparison: Compare and contrast PrP C and PrP Sc structures and physical properties, and describe prion "infection" mechanisms in Creutzfeldt-Jakob Disease (CJD). Note the misfolding of a normal protein (PrP C) into a pathogenic form (PrP Sc).

    • CJD vs. Alzheimer's Disease (AD): Compare and contrast key features of CJD and Alzheimer's disease (AD). Mention accumulation of misfolded proteins as a commonality.

    • Hsp70 and Hsp60: Define Hsp70 and Hsp60, providing examples for each, and illustrating their different modes of action. Explain their role in preventing protein misfolding and aggregation. Describe examples.

    Enzyme Kinetics (Additional Points - not explicitly covered in the reading assignments, but potentially helpful)

    • Michaelis-Menten Kinetics: Calculate Vmax and KM using the Michaelis-Menten model (hyperbole) and the Lineweaver-Burk model.

    • Enzyme Inhibitors: Compare and contrast competitive and noncompetitive inhibitors, describing effects on KM and Vmax. Explain how inhibitors can affect enzyme function and activity.

    • Antibiotic Mechanisms: Describe mechanisms of action of three common types of antibiotics targeting bacterial cell walls, protein synthesis, and specific bacterial enzymes. (More specific detail will depend on the exact antibiotics the text covers.)

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    Description

    This quiz covers fundamental concepts in cell and molecular biology. Students will explore diagrams of prokaryotic, plant, and animal cells, as well as the tenets of Cell Theory and significant contributions by scientists like Lynn Margulis. Additionally, it examines the evidence supporting the endosymbiotic theory, focusing on the origins of mitochondria and chloroplasts.

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