Definitions of Life and Molecules
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Questions and Answers

What is the primary factor determining the primary structure of a protein?

  • The availability of essential amino acids in the diet.
  • The DNA sequence that codes for the protein. (correct)
  • The presence of chaperones during folding.
  • The pH and temperature of the cellular environment.
  • Which level of protein structure is stabilized by hydrogen bonds between backbone atoms, resulting in structures like alpha-helices and beta-pleated sheets?

  • Primary
  • Tertiary
  • Secondary (correct)
  • Quaternary
  • What type of interaction is NOT a main force that holds the tertiary structure of a protein together?

  • Peptide bond (correct)
  • Salt bridges
  • Disulfide bond
  • Hydrophobic interactions
  • Which of the following best describes the quaternary structure of a protein?

    <p>The arrangement of multiple folded protein subunits into a multi-subunit complex. (D)</p> Signup and view all the answers

    What is the most likely consequence of protein denaturation?

    <p>Disruption of secondary, tertiary, and quaternary structures (C)</p> Signup and view all the answers

    Which type of protein is NOT fixed to one spot in the body and is involved in transport or signaling?

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

    What is the primary function of serum albumins in blood plasma?

    <p>Maintenance of osmotic pressure and transport of nonpolar substances (A)</p> Signup and view all the answers

    Unlike blood plasma proteins, where is hemoglobin primarily located?

    <p>Red blood cells (D)</p> Signup and view all the answers

    How does insulin affect glucose uptake by cells?

    <p>It signals the translocation of GLUT4 transporter proteins to the cell membrane. (A)</p> Signup and view all the answers

    What is the function of somatropin in the human body?

    <p>Promotes protein synthesis, increase in muscle cells, and bone growth. (C)</p> Signup and view all the answers

    Which structural feature is characteristic of collagen?

    <p>Three strands of procollagen cross-linked via hydrogen bonds (D)</p> Signup and view all the answers

    Where is elastin particularly important in the human body?

    <p>Arteries, lungs, skin, and elastic ligaments/cartilage (C)</p> Signup and view all the answers

    What is a key characteristic of proteoglycans?

    <p>They consist of a core protein with many polar carbohydrate (CHO) side chains. (D)</p> Signup and view all the answers

    What is the main function of fibronectin?

    <p>To crosslink other matrix proteins such as collagen and proteoglycans (B)</p> Signup and view all the answers

    What percentage of total dietary intake should proteins comprise?

    <p>10-35% (C)</p> Signup and view all the answers

    Which of the following is the most accurate description of homeostasis in living organisms?

    <p>The regulation of internal conditions to maintain a stable environment. (A)</p> Signup and view all the answers

    Which statement best explains the relationship between catabolism and anabolism?

    <p>Catabolism breaks down complex molecules to release energy used in anabolism to synthesize new ones. (C)</p> Signup and view all the answers

    Why is carbon considered the basis of life on Earth?

    <p>It can form stable bonds with many other elements, including itself, allowing for diverse and complex molecules. (C)</p> Signup and view all the answers

    How does the first law of thermodynamics apply to living organisms?

    <p>Living organisms convert energy from one form to another without creating or destroying it. (A)</p> Signup and view all the answers

    What role does ATP play in living organisms?

    <p>It acts as the common energy currency for cellular processes. (A)</p> Signup and view all the answers

    What distinguishes a micronutrient from a macronutrient?

    <p>Micronutrients are required in small amounts, while macronutrients are required in large amounts. (A)</p> Signup and view all the answers

    How does RNA differ structurally from DNA?

    <p>RNA is single-stranded and uses uracil instead of thymine. (D)</p> Signup and view all the answers

    Which type of hydrocarbon contains at least one carbon-carbon double bond?

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

    An atom has 6 electrons in its outermost shell. How many more electrons does it need to fill this shell and what type of bonds is it most likely to form?

    <p>Needs 2 more electrons; likely to form covalent bonds. (A)</p> Signup and view all the answers

    Which of the following best describes the relative strength of intermolecular bonds compared to intramolecular bonds?

    <p>Intermolecular bonds are weaker and require less energy to break. (D)</p> Signup and view all the answers

    How does electronegativity influence the formation of polar covalent bonds?

    <p>High electronegativity differences lead to unequal sharing of electrons, resulting in polar covalent bonds. (B)</p> Signup and view all the answers

    Why do hydrophobic molecules tend to cluster together in an aqueous solution?

    <p>They are repelled by water molecules and seek each other out. (B)</p> Signup and view all the answers

    How does an acid affect the pH of water?

    <p>Acids act as proton donors, increasing the concentration of hydronium ions, which lowers the pH. (D)</p> Signup and view all the answers

    What distinguishes spatial isomers from structural isomers?

    <p>Spatial isomers have the same bonding arrangement but different spatial positioning of atoms, while structural isomers have differing bonds between atoms. (C)</p> Signup and view all the answers

    In the context of thermodynamics, what does a negative $\Delta$G (Gibbs free energy) indicate about a reaction?

    <p>The reaction releases energy and is spontaneous. (C)</p> Signup and view all the answers

    Flashcards

    Organization

    Being composed of one or more cells, vital units of life.

    Metabolism

    The chemical processes necessary for maintaining life, including catabolism and anabolism.

    Homeostasis

    Regulation of the internal environment to maintain stability, like temperature control.

    Response to Stimuli

    The ability of life forms to react to environmental changes.

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    ATP

    Adenosine triphosphate, the common energy currency of life.

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    Macronutrients

    Nutrients required in large amounts, such as carbs and proteins.

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    Micronutrients

    Nutrients needed in small amounts, like vitamins and minerals.

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    Covalent Bonds

    Bonds formed by the sharing of electron pairs between atoms.

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    Ionic Bonds

    Bonds formed when electrons are transferred from one atom to another.

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    Hydrogen Bonds

    Weak attractions between a hydrogen atom in one molecule and an electronegative atom in another.

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    Entropy

    A measure of disorder or randomness in a system; higher entropy means less energy.

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    Gibbs Free Energy

    The maximum amount of energy available to do work in a system, expressed as ΔG.

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    Exergonic Reactions

    Reactions that release energy and occur spontaneously, having a negative ΔG.

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    Endergonic Reactions

    Reactions that absorb energy, occurring non-spontaneously with a positive ΔG.

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    Nutrients

    Substances vital to an organism’s growth, maintenance, and repair, providing energy or building blocks.

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    Basal Metabolic Rate (BMR)

    Rate of energy expenditure at rest; calories burned in 24 hours.

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    Thermic Effect of Food (TEF)

    Calories burned through digesting and processing food.

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    Essential Amino Acids

    Amino acids that must be obtained through diet; 9 out of 20.

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    Dipeptide

    A molecule formed from 2 amino acids joined by a peptide bond.

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    Polypeptide

    A chain of >50 amino acids linked together.

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    Quaternary Structure

    Combination of multiple folded protein subunits.

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    Denaturation

    The process that disrupts protein structure, affecting its function.

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    Dynamic Proteins

    Proteins that move and perform functions throughout the body.

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    Static Proteins

    Proteins that remain fixed at specific sites in the body.

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    Hemoglobin

    Protein in red blood cells that carries oxygen.

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    Myoglobin

    Oxygen-binding protein in muscle cells.

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    Insulin

    Hormone that regulates blood glucose levels by enabling cellular uptake.

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    Collagen

    Most abundant protein in mammals, provides structural support.

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    Actin

    Protein that forms thin filaments in muscle cells.

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    Proteoglycans

    Molecules made of a core protein and polysaccharide chains, important in tissues.

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    Study Notes

    Conventional Definitions of Life

    • Organization: Composed of one or more cells, the basic units of life.
    • Reproduction: Ability to produce new organisms.
    • Metabolism: Chemical processes necessary for life maintenance.
      • Catabolism: Breaking down substances to release energy.
      • Anabolism: Synthesizing substances using energy.
    • Growth: Increased complexity from simpler to more complex forms.
    • Homeostasis: Maintaining a constant internal environment.
      • Examples: Sweating to reduce temperature, shivering to increase temperature.
    • Response to Stimuli: Ability to react to a stimulus.
    • Adaptation: Ability to respond over time to environmental changes.

    Other Proposed Features of Life

    • Carbon Containing: Carbon forms the foundation of life on Earth.
    • Reliance on Water: Water is essential for all life forms.
    • Genetic Information: Uses DNA and RNA to store the blueprint for an organism.

    What is a Molecule?

    • Molecule: Smallest particle of a substance retaining its properties.
    • Atom: Smallest particle of an element retaining its chemical properties; a molecule may be composed of one or more atoms

    Molecular Characteristics of Life

    • Thermodynamics: Life obeys the laws of thermodynamics.
    • ATP: Common energy currency of life.
    • Biological Molecules: Structure depends on similar biological molecules (e.g., proteins, lipids, carbohydrates, nucleic acids).

    What is a Nutrient?

    • Nutrient: Substance with nutritional value for an organism.
    • Micronutrients: Required in small amounts (vitamins, microminerals).
    • Macronutrients: Required in large amounts (carbohydrates, proteins, lipids).

    Vitamins

    • Act as cofactors for enzymes, and are organic compounds loosely bound to the enzyme during chemical reactions.

    Nucleic Acids

    • Essential for maintaining, growing, and repairing DNA and RNA.
    • RNA is a messenger that carries instructions from DNA.
    • RNA uses uracil instead of thymine.
    • RNA is single-stranded.

    Hydrocarbon Nomenclature

    • Hydrocarbons: Chemical compounds containing only hydrogen and carbon.
    • Alkane: Carbon-carbon single bonds.
    • Alkene: At least one carbon-carbon double bond.
    • Alkyne: At least one carbon-carbon triple bond.

    Methods of Drawing Hydrocarbons

    • Structural: Straight lines represent bonds.
    • Condensed: Combines hydrogen atoms with carbons for simpler representation.
    • Skeletal: Intersections represent carbon atoms.

    Naming Linear Hydrocarbons

    • Use prefixes to name hydrocarbons according to the number of carbon atoms present.

    Atomic Structure

    • Atoms have a central nucleus with protons and neutrons, with electrons orbiting around the nucleus.
    • The number of protons defines the element.

    Bond Formation by Atoms

    • Atoms form bonds to fill their outermost electron shell.
    • Number of bonds formed depends on the number of electrons needed to fill or empty the outermost partially filled orbital

    Number of Bonds Formed by Bioelements

    List of elements and the number of bonds formed by each.

    Chemical Bonds

    • Types of Chemical Bonds -Intramolecular(covalent and ionic bonds) within a molecule. -Intermolecular (hydrogen bonds, Van der Waals forces, hydrophilic interactions) between molecules.

    Relative Chemical Bond Strengths

    • Intramolecular bonds require more energy to form but also release more energy when broken compared to intermolecular ones.

    Covalent Bonds

    • Sharing of electrons between atoms resulting in stable bonds.

    Ionic Bonds

    • Transfer of electrons between atoms resulting in oppositely charged ions that attract each other.

    Hydrogen Bonds

    • Attraction between hydrogen and another highly electronegative atom.

    Van der Waals Forces

    • Temporary electrostatic attraction between molecules.

    Electronegativity and Polarity

    • Electronegativity is the ability of an atom to attract electrons.
    • Polarity arises from unequal sharing of electrons.
    • Bond polarity is determined by the difference in electronegativity.

    Polar Bonds vs Polar Molecules

    • A polar bond is within a molecule.
    • Polar molecules involve multiple polar bonds and the overall shape of the molecule.

    Water Properties

    • Water is a polar molecule.
    • Oxygen has a partial negative charge, and hydrogen atoms have partial positive charges.

    Importance of Polarity in Solubility

    • Polar substances dissolve in polar solvents, and nonpolar substances dissolve in nonpolar solvents.

    Acids and Bases

    • Acids are proton donors.
    • Bases are proton acceptors.

    Isomers

    • Isomers have the same molecular formula but different atomic arrangements.

    Structural Isomers

    • Different bonding arrangements between atoms.

    Spatial Isomers

    • Same bonding arrangement, but different spatial positioning of atoms.

    Energy in Biochemistry

    • Energy is transferred between molecules in chemical reactions.
    • Change in enthalpy measures the heat change in reactions (delta H).
    • Exergonic reactions release energy (delta H negative).
    • Endergonic reactions require energy input (delta H positive).

    Negative delta H - Exothermic

    Loss of heat, energy released, Final product temp less than initial reactant temp

    Positive delta H - Endothermic

    Gain of heat , energy absorbed, Final product temp more than initial reactant temp

    Negative Delta G - Spontaneous Reaction

    • The reaction will proceed spontaneously.

    Spontaneous Reactions:

    Reactions occur naturally without external influence

    What else determines if a reaction is possible?

    Entropy and second law of thermodynamics factors.

    Entropy

    • Measure of disorder or randomness in a system.
    • Higher entropy means more disorder.
    • Reactions tend toward higher entropy.

    Gibbs Free Energy

    • Combines enthalpy and entropy changes.

    Exergonic vs Endergonic Reactions

    Exergonic reactions release energy; Endergonic reactions require energy.

    Conditions Favouring Exergonic Reactions

    • Reactions that lose heat and gain entropy are energetically favorable

    DeltaG vs DeltaG°

    • delta G is the actual free energy change under specific conditions.
    • DeltaG° is under standard conditions (298k, 1atm, 1M concentration)

    Energy in Food - Gross Energy

    • Gross energy is the total energy in food.
    • Energy is released by combustion or oxidation.

    Useable Energy

    Energy for organismic functions such as growth, maintenance, and reproduction

    Energy Out

    Expenditures over 24hrs, including Basal Metabolic Rate (BMR) and Thermic Effect of Food (TEF), and activity level.

    3 factors affecting Obesity Epidemics

    Intake of fast food, added sugar, and large portion sizes.

    Amino Acids

    Building blocks of protein, with 20 standard amino acids, some essential in the diet.

    Protein Peptides

    • Amino acids linked by peptide bonds into chains, from dipeptides to oligopeptides (short chains) to larger polypeptides that constitute proteins.

    Protein Polymers

    Polypeptides that are larger (more than 50 aa)

    Biological Proteins

    Proteins (hundreds to thousands of amino acids) function in various biological roles, in different, complex structures

    Protein Structure Levels

    Levels of protein structure include primary, secondary, tertiary, and quaternary structures

    Structure of Proteins (Detail)

    Describes polypeptide sequence order, interactions amongst amino acids for secondary structures (alpha helices, beta sheets), 3D folding for tertiary structures, and interactions of multiple polypeptide subunits in quaternary structures. Includes different forces holding structures together (hydrogen bonds, disulfide bonds etc)

    Dynamic vs Static Proteins

    • Dynamic proteins are not fixed in one spot in the body. Ex: transporter proteins, enzymes
    • Static proteins are fixed to one location in the body. Ex: collagen, actin/myosin

    Serum Albumins

    • Water-soluble proteins (60% of plasma proteins).
    • Maintain osmotic pressure.

    Globulins

    • Water-soluble proteins (40% of plasma proteins).
    • Transport, binding, and eliminating foreign particles

    Hemoglobin

    • Protein in red blood cells.
    • Transports oxygen.

    Myoglobin

    • Protein in muscle cells.
    • Stores oxygen.

    Insulin

    • Hormone controlling blood glucose levels.

    Thyroid Hormones (T3 and T4).

    • Produced in thyroid gland.
    • Regulate metabolism and growth.

    Somatotropin

    • Growth hormone produced in the pituitary gland.
    • Stimulates growth and development

    Collagen

    • Structural protein in connective tissues.
    • Abundant in mammals.

    Elastin

    • Flexible protein in connective tissues (skin, ligaments, blood vessels.

    Proteoglycans

    • Proteins with carbohydrate chains.
    • Important components of connective tissues.

    Fibronectin

    Extracellular matrix protein.

    Actin and Myosin

    Proteins involved in muscle contraction

    Dietary Protein

    • Dietary protein intake: 10-35%.
    • Essential AA synthesis by body: 10-12.

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