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General Biology: Carbon and Molecular Diversity of Life

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Termini in questo insieme (30)

  • Most abundant element in living systems excluding water
    Carbon is the most abundant element in living systems after excluding water.
  • Definition of organic molecules
    Organic molecules contain covalently linked carbon and hydrogen atoms.
  • What are hydrocarbons?
    Hydrocarbons are organic molecules made only of carbon and hydrogen atoms.
  • Why is carbon an excellent building block?
    Carbon forms four covalent bonds, allowing flexible molecular structures with variations in length, double bond position, branching, and ring formation.
  • What are functional groups?
    Functional groups are reactive groups of atoms commonly found attached to carbon backbones that determine molecule properties.
  • Primary classes of biomolecules
    The four primary biomolecule classes are carbohydrates, proteins, nucleic acids, and lipids.
  • Difference between monomers and polymers
    Monomers are individual building blocks; polymers are long chains of monomers linked covalently.
  • What is dehydration synthesis?
    Dehydration synthesis forms covalent bonds between monomers by removing water, building polymers.
  • What is hydrolysis?
    Hydrolysis breaks covalent bonds in polymers by adding water, releasing monomers.
  • General formula of simple carbohydrates
    Simple carbohydrates fit the formula \(C_n(H_2O)_n\), e.g., glucose.
  • Three size classes of carbohydrates
    Monosaccharides (single units), disaccharides (2-~10 units), and polysaccharides (20+ units).
  • Bond linking monosaccharides
    Monosaccharides are linked by glycosidic bonds formed via dehydration synthesis.
  • Two main functions of carbohydrates
    Carbohydrates provide structural support (e.g., cellulose) and energy storage (e.g., starch, glycogen).
  • Monomers of proteins
    Proteins are polymers made of amino acid monomers.
  • Covalent bond linking amino acids
    A peptide bond covalently links adjacent amino acids.
  • Four levels of protein structure
    Primary (amino acid sequence), secondary (alpha helices/beta sheets), tertiary (3D shape), quaternary (multiple polypeptides).
  • What causes protein denaturation?
    Environmental changes like heat, pH, or salt concentration can cause proteins to lose their functional shape.
  • Role of chaperone proteins
    Chaperones assist in protein folding and help denatured proteins regain their proper shape.
  • Monomers of nucleic acids
    Nucleic acids are polymers of nucleotides.
  • Three components of a nucleotide
    A nucleotide consists of a phosphate group, a pentose sugar, and a nitrogenous base.
  • Difference between DNA and RNA sugars
    DNA contains deoxyribose (lacking one hydroxyl group), RNA contains ribose.
  • Two groups of nitrogenous bases
    Pyrimidines (single-ring: cytosine, thymine, uracil) and purines (double-ring: adenine, guanine).
  • Base pairing in DNA
    Adenine pairs with thymine, and cytosine pairs with guanine via hydrogen bonds.
  • Bond linking nucleotides
    Nucleotides are linked by phosphodiester bonds formed by dehydration synthesis.
  • DNA structure
    DNA is a double helix with two antiparallel strands connected by base-pair hydrogen bonds.
  • Definition of lipids
    Lipids are hydrophobic biomolecules that do not form polymers and include fats, phospholipids, steroids, and waxes.
  • Difference between saturated and unsaturated fatty acids
    Saturated fatty acids have only single C-C bonds and are solid at room temperature; unsaturated have one or more C=C double bonds causing kinks and are liquid.
  • Structure of triglycerides
    Triglycerides consist of three fatty acid chains covalently linked to a glycerol molecule.
  • Phospholipid structure and function
    Phospholipids have hydrophilic heads and hydrophobic tails and are major components of cell membranes.
  • Role of steroids and waxes
    Steroids have fused carbon rings important for membrane structure; waxes protect and prevent water loss.