AP Biology Unit 1 Study Guide: Chemistry of Life

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Vocabulary practice flashcards covering chemical bonds, elements of life, functional groups, properties of water, biomolecules, and protein folding from the AP Biology Unit 1 Study Guide.

Last updated 10:18 PM on 10/12/26
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41 Terms

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Electronegativity

An atom's capacity to pull shared electrons toward itself in a chemical bond, determined by atomic number, valence electron distance from the nucleus, and electron tendency.

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Covalent Bond

A strong, difficult-to-break chemical bond formed by the sharing of valence electrons between atoms; forms the structural backbones of organic macromolecules.

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Nonpolar Covalent Bond

A bond formed by equal electron sharing due to similar electronegativities, producing no partial charges; found in hydrophobic regions and molecules such as C−HC-H and O=OO=O.

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Polar Covalent Bond

A bond characterized by unequal electron sharing due to higher electronegativity in one atom, generating partial charges (δ+\delta^+, δ−\delta^-); found in hydrophilic regions and molecules such as O−HO-H and N−HN-H.

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Ionic Bond

A chemical bond resulting from the transfer of electrons to create oppositely charged ions that attract; strong in dry crystals but dissociates in aqueous environments.

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Hydrogen Bond

An attraction between a partially positive hydrogen (δ+\delta^+) and an electronegative atom (δ−\delta^-) on another molecule or region; weak individually but strong in high numbers.

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Organic Molecule

A chemical compound containing carbon-to-hydrogen (C−HC-H) bonds.

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Inorganic Molecule

A chemical compound lacking carbon-to-hydrogen (C−HC-H) bonds.

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Functional Groups

Specific clusters of atoms attached to carbon skeletons that dictate a molecule's chemical behavior.

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Hydroxyl Group

A polar functional group with the structure −OH-OH.

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Methyl Group

A nonpolar functional group with the structure −CH3-CH_3.

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Carbonyl Group

A polar functional group featuring a carbon double-bonded to an oxygen atom (C=OC=O).

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Carboxyl Group

A charged, acidic functional group (−COOH-COOH) that ionizes to release H+H^+.

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Amino Group

A charged, basic functional group (−NH2-NH_2) that ionizes to accept H+H^+.

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Phosphate Group

A charged, acidic functional group containing phosphorus bonded to oxygen atoms that ionizes to release H+H^+.

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Sulfhydryl Group

A polar functional group with the structure −SH-SH.

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Cohesion

The intermolecular attraction between identical water molecules via hydrogen bonding.

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Surface Tension

A measure of the difficulty in stretching or breaking the surface of a liquid; highly elevated in water due to cohesive hydrogen bonding.

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Adhesion

The attraction of water molecules to other polar surfaces.

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Capillary Action

The upward movement of water in narrow spaces combining cohesion and adhesion, seen in plant xylem and capillary tubes.

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High Specific Heat

The amount of heat that must be absorbed or lost for 1 g1\,g of a substance to change temperature by 1∘C1^\circ\text{C}; in water, heat is initially absorbed to break hydrogen bonds before molecules move faster.

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High Heat of Vaporization

The amount of energy required to convert 1 g1\,g of liquid into gas.

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Evaporative Cooling

The process by which the surface of an object cools during evaporation as the highest-energy water molecules transition into gas (e.g., sweating, panting, transpiration).

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Density of Ice

The physical property wherein solid water is ~10%10\% less dense than liquid water because hydrogen bonds below 4∘C4^\circ\text{C} lock into a stable, rigid crystalline lattice holding molecules farther apart.

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Hydration Shell

A sphere of water molecules surrounding dissolved ions through partial charge interactions.

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Hydrophilic

Substances that are polar or charged and readily dissolve in water (e.g., salts, sugars, polar amino acids).

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Hydrophobic

Nonpolar substances that do not dissolve in water because water molecules preferentially form hydrogen bonds with each other (e.g., lipids, steroids).

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Monomer

A single repeating subunit used as a building block to synthesize polymers.

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Polymer

A long chain of monomers linked together by covalent bonds.

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Dehydration Synthesis

An energy-requiring reaction that joins monomers into polymers by removing H2OH_2O (one monomer loses −OH-OH, the other loses −H-H) to form a covalent bond.

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Hydrolysis

An energy-releasing reaction that breaks covalent bonds in polymers to produce monomers by adding H2OH_2O, splitting it into −OH-OH and −H-H attached to adjacent subunits.

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Carbohydrate

A biomolecule composed of Carbon (CC), Hydrogen (HH), and Oxygen (OO), formed from monosaccharide monomers and polysaccharide polymers, providing fast energy and structural cellulose in plant cell walls.

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Lipid

A biomolecule composed of Carbon (CC), Hydrogen (HH), Oxygen (OO), and sometimes phosphorus (PP); lacks a true monomer or polymer and functions in cell membranes, long-term energy storage, thermal insulation, and hormones.

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Protein

A biomolecule composed of Carbon (CC), Hydrogen (HH), Oxygen (OO), Nitrogen (NN), and sometimes sulfur (SS), consisting of amino acid monomers joined into polypeptide chains.

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Nucleic Acid

A biomolecule composed of Carbon (CC), Hydrogen (HH), Oxygen (OO), Nitrogen (NN), and Phosphorus (PP), consisting of nucleotide monomers that assemble into DNA and RNA to store and transmit genetic information.

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Phosphodiester Bond

The covalent bond that links nucleotide monomers together along a nucleic acid strand.

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Primary Structure (1∘1^\circ)

The specific, linear sequence of amino acids in a polypeptide chain encoded directly by DNA.

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Secondary Structure (2∘2^\circ)

Localized hydrogen bonding along the polypeptide backbone that forms α\alpha-helices and β\beta-pleated sheets.

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Tertiary Structure (3∘3^\circ)

The overall three-dimensional shape of a polypeptide resulting from R-group interactions, including hydrophobic clustering, hydrogen bonds, ionic bonds, and covalent disulfide bridges.

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Quaternary Structure (4∘4^\circ)

The structural association formed by two or more independent polypeptide subunits joining together (e.g., hemoglobin, collagen).

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Denaturation

The disruption of a protein's secondary (2∘2^\circ), tertiary (3∘3^\circ), and quaternary (4∘4^\circ) structure caused by changes in temperature, pHpH, salinity, or chemicals, leading to loss of biological function.