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General Biology: Key Concepts in Water, Elements, Macromolecules, and Biomolecules

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  • What causes water's polarity?
    Oxygen pulls shared electrons harder than hydrogen, creating an uneven charge.
  • What is a hydrogen bond?
    A weak attraction between a positive hydrogen atom and a negative atom in another molecule.
  • What allows water to hydrogen bond?
    Its polar covalent bonds and bent shape.
  • Name properties of water due to its polarity.
    Cohesion, adhesion, high specific heat, surface tension, and excellent dissolving abilities.
  • Difference between cohesion and adhesion?
    Cohesion is water sticking to water; adhesion is water sticking to other surfaces.
  • Why does water have high surface tension?
    Hydrogen bonds pull surface molecules tightly together, making it hard to break the surface.
  • What does high heat capacity of water mean?
    It takes a large amount of heat energy to change water's temperature.
  • What is evaporative cooling?
    The surface cools as the hottest liquid molecules evaporate away as gas.
  • Why is water a good solvent?
    Its polar charges attract and break apart ionic and polar substances.
  • Difference between hydrophilic and hydrophobic?
    Hydrophilic means water-loving (dissolves); hydrophobic means water-fearing (does not dissolve).
  • What 4 major elements make up most living organisms?
    Carbon, Hydrogen, Oxygen, and Nitrogen (CHON).
  • What defines an organic compound?
    It contains carbon bonded to hydrogen (C-H bonds).
  • Why is carbon important for building molecules?
    It has four valence electrons, allowing four stable covalent bonds.
  • What are trace elements and their importance?
    Elements needed in tiny amounts (like iron); essential for survival.
  • What are the 4 classes of biomacromolecules?
    Carbohydrates, Lipids, Proteins, and Nucleic Acids.
  • Difference between monomer and polymer?
    A monomer is a single building block; a polymer is a long chain of monomers.
  • Which macromolecules follow monomer-polymer format?
    Carbohydrates, Proteins, and Nucleic Acids (Lipids do not).
  • What does dehydration synthesis do?
    Connects monomers into polymers by removing a water molecule.
  • What is hydrolysis?
    Splitting apart polymers into monomers by adding a water molecule.
  • Define carbohydrate and its types.
    Sugars used for energy and structure; types include monosaccharides, disaccharides, and polysaccharides.
  • What elements are in carbohydrates?
    Carbon, Hydrogen, and Oxygen (CHO).
  • Typical element ratio in monosaccharides?
    1:2:1 ratio of Carbon:Hydrogen:Oxygen (CH₂O).
  • What bond links two monosaccharides?
    A glycosidic linkage formed by dehydration synthesis.
  • Difference between branched and unbranched polysaccharides?
    Branched have side-chains for fast energy release; unbranched form straight fibers for structure.
  • How are lipids different from other macromolecules?
    They are not true polymers and are highly hydrophobic.
  • What are the two major components of lipids?
    Glycerol and fatty acids.
  • What bond connects fatty acids to glycerol?
    An ester linkage.
  • Difference between saturated and unsaturated fatty acids?
    Saturated have no double bonds (straight); unsaturated have one or more double bonds (kinked).
  • What is a phospholipid and its function?
    A lipid with one hydrophilic head and two hydrophobic tails; forms cell membrane bilayers.
  • What is the function of nucleic acids?
    To store and transmit genetic information.
  • What is the monomer of nucleic acids?
    A nucleotide composed of sugar, phosphate group, and nitrogenous base.
  • How do nitrogenous bases pair in DNA?
    Adenine pairs with Thymine (A-T); Guanine pairs with Cytosine (G-C).
  • Differences between DNA and RNA?
    DNA is double-stranded with deoxyribose and Thymine; RNA is single-stranded with ribose and Uracil.
  • What are proteins made of?
    Amino acids linked by peptide bonds.
  • What determines amino acid properties?
    The R group (side chain).
  • Describe the four levels of protein structure.
    Primary: amino acid sequence; Secondary: coils/pleats; Tertiary: 3D shape; Quaternary: multiple chains.
  • What is denaturation?
    Protein unfolding due to environmental factors, causing loss of function.