AP Biology · 12 free flashcards

Chemistry of life flashcards

The key ideas of chemistry of life for AP Biology, as flashcards you can study with spaced repetition.

What you need to know

The chemistry of life covers the atomic and molecular foundations that make biology possible. Students must understand how water's unique properties arise from hydrogen bonding and polarity, enabling life as a solvent and temperature buffer. Carbon's ability to form four covalent bonds allows the enormous diversity of organic molecules. The four major macromolecules, carbohydrates, lipids, proteins, and nucleic acids, are built through dehydration synthesis and broken down by hydrolysis. Each macromolecule has a distinct monomer, structure, and function. Proteins are especially complex, with four levels of structure that determine function. Enzymes are biological catalysts whose activity depends on pH, temperature, and substrate concentration. Understanding how molecular structure relates to biological function is the central theme throughout this topic.

Chemistry of life: 12 key flashcards

  1. Card 1

    Why is water considered a polar molecule?

    Oxygen is more electronegative than hydrogen, so electrons are pulled toward oxygen, creating partial negative and positive charges across the molecule.
  2. Card 2

    How does hydrogen bonding explain water's high specific heat?

    Hydrogen bonds between water molecules absorb large amounts of energy before temperature rises, resisting rapid temperature changes and stabilizing aquatic environments.
  3. Card 3

    What is the difference between dehydration synthesis and hydrolysis?

    Dehydration synthesis joins monomers by removing water; hydrolysis breaks polymers apart by adding water, splitting covalent bonds between subunits.
  4. Card 4

    What property makes carbon the backbone of organic molecules?

    Carbon can form four covalent bonds, allowing it to create chains, branches, and rings, producing the vast structural diversity needed for life's molecules.
  5. Card 5

    What are the monomers of proteins, and what bonds link them?

    Amino acids are the monomers of proteins, linked together by peptide bonds formed between the amino group of one and the carboxyl group of the next.
  6. Card 6

    What level of protein structure is determined by hydrogen bonds between backbone atoms?

    Secondary structure, including alpha helices and beta pleated sheets, results from hydrogen bonds between atoms of the polypeptide backbone, not the side chains.
  7. Card 7

    How do phospholipids form a bilayer in cell membranes?

    Phospholipids have a hydrophilic phosphate head and hydrophobic fatty acid tails; in water, tails face inward and heads face outward, forming a stable bilayer.
  8. Card 8

    What is the monomer of nucleic acids, and what three parts does it contain?

    The monomer is a nucleotide, consisting of a five-carbon sugar, a phosphate group, and a nitrogenous base bonded together.
  9. Card 9

    How do saturated and unsaturated fatty acids differ structurally?

    Saturated fatty acids have only single bonds and are straight, packing tightly; unsaturated fatty acids have one or more double bonds, causing kinks that reduce packing.
  10. Card 10

    What is an enzyme's active site, and how does it relate to substrate specificity?

    The active site is a specific region of the enzyme whose shape complements the substrate, explaining specificity through the induced fit model of enzyme-substrate interaction.
  11. Card 11

    What role do functional groups play in organic molecules?

    Functional groups such as hydroxyl, carboxyl, and amino groups determine the chemical properties and reactivity of organic molecules, influencing how they interact with other molecules.
  12. Card 12

    Why do high temperatures denature proteins?

    Excess heat disrupts the weak interactions such as hydrogen bonds and van der Waals forces that maintain tertiary structure, causing the protein to unfold and lose function.

Quick quiz

Question 1 of 3

A researcher adds a competitive inhibitor to an enzyme reaction. Which outcome best describes the effect on enzyme activity?

Common mistakes

  • Many students confuse dehydration synthesis with hydrolysis, incorrectly stating that water is released during the breakdown of polymers rather than during their assembly.
  • Students often assume that lipids are always solid fats, overlooking that unsaturated lipids such as oils are liquid at room temperature due to double bonds creating kinks that prevent tight packing.
  • A frequent error is claiming that enzymes are consumed or permanently altered during a reaction, when in reality enzymes are biological catalysts that are released unchanged after each reaction cycle.

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Written for general AP revision. Exam boards and schools differ, so check your own specification for exactly what you need to know. Lerno is not affiliated with any exam board.