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Honors Biology Unit 2 Review: Biochemistry - The Chemistry of Life

Unit 2 covers the chemistry underneath every living thing, from how atoms bond and why water behaves so strangely to how enzymes speed up reactions in your cells. After this unit, you should be able to explain how a molecule's structure determines its job, whether that molecule is water, a fat, a protein, or an enzyme.

Read the overview for the big picture, then work through the review notes in order and answer each checkpoint question before checking the answer.

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What is Honors Biology unit 2?

Biology runs on chemistry. This unit gives you the vocabulary and models you'll use in every later unit, including cell membranes, DNA replication, and photosynthesis.

Honors Biology Unit 2 covers biochemistry, the chemistry that makes life possible. You study the properties of water and how they come from hydrogen bonding. You also learn how atoms form covalent, ionic, and hydrogen bonds. The unit covers the four classes of organic macromolecules (carbohydrates, lipids, proteins, and nucleic acids) and how cells build and break them down. Finally, you learn how enzymes lower activation energy to speed up reactions. Expect calculations like specific heat problems and data questions that graph enzyme activity against temperature or pH. Topic order varies by school, and some courses teach atoms and bonds before water.

Water's polarity explains almost all of its life-supporting properties.

Oxygen hogs electrons, so water has a slightly negative end and two slightly positive ends. Those partial charges let water molecules hydrogen bond to each other. Hydrogen bonding produces cohesion, adhesion, high specific heat, and floating ice. Polarity also lets water dissolve ions and polar molecules.

Big biological molecules are built from small repeating units.

In a dehydration synthesis model, joining monomers releases one water molecule per bond formed. Hydrolysis breaks those bonds by adding water. Cells can also use activated building blocks to make polymers through reactions that do not directly release water. Glucose builds starch, amino acids build proteins, and nucleotides build DNA. Lipids are the exception because they aren't true polymers.

An enzyme works only as long as it keeps its shape.

Enzymes speed reactions by lowering activation energy. Their active sites bind specific substrates, and some enzymes bind more than one substrate. Heat or extreme pH can change an enzyme's shape, while inhibitors can reduce its activity in different ways.

Structure determines function, all the way down to the atom.

The arrangement of electrons decides whether a bond is polar. Polarity decides whether a molecule mixes with water. The way a protein folds decides whether it can catalyze a reaction. If you can trace a property back to structure, you understand the unit.

Honors Biology unit 2 topics

Unit 2 review notes

2.1

Water and Its Properties

Water is polar. Oxygen pulls shared electrons harder than hydrogen does, so the oxygen end carries a partial negative charge (δ−\delta^-) and each hydrogen carries a partial positive charge (δ+\delta^+). Water's bent shape keeps those charges on opposite sides of the molecule.

Polarity lets neighboring water molecules form hydrogen bonds. A hydrogen bond is a weak attraction between a hydrogen on one molecule and the oxygen on another. One hydrogen bond is weak, but water forms huge numbers of them.

Cohesion (water sticking to water) creates surface tension strong enough to hold up a water strider. Adhesion (water sticking to other surfaces) works with cohesion to move water up narrow xylem tubes in plants. Water dissolves ions and polar molecules, so most cell reactions happen in it. Ice floats because hydrogen bonds lock frozen molecules into an open lattice that is less dense than liquid water. As a result, lakes freeze from the top and fish survive underneath.

Worked example. How much energy does it take to warm 200 g of water from 20°C to 25°C? Use q=mcΔTq = mc\Delta T with water's specific heat of 4.18 J/g°C. Then q=(200)(4.18)(5)=4180q = (200)(4.18)(5) = 4180 J. Warming 200 g of iron (0.45 J/g°C) the same amount takes only about 450 J. That gap explains why oceans and your body resist fast temperature swings.

  • Hydrogen bond: A weak attraction between a partially positive hydrogen on one molecule and a partially negative atom, like oxygen, on another.
  • Cohesion: The attraction of water molecules to each other, which causes surface tension.
  • Adhesion: The attraction of water molecules to other surfaces, such as glass or the walls of xylem.
  • Specific heat: The energy needed to raise 1 gram of a substance by 1°C, which is 4.18 J for water.

Check yourself: Why does sweating cool you down? (Answer: Water has a high heat of vaporization. Each gram of sweat that evaporates must break many hydrogen bonds, and it carries that heat energy away from your skin.)

2.2

Atoms, Molecules, and Chemical Bonds

An atom has protons and neutrons in its nucleus and electrons outside it. The number of protons is the atomic number, and it sets the element's identity. Every carbon atom has 6 protons.

Neutron counts can vary, and these variants are called isotopes. Carbon-14 has a mass number of 14, so it has 14−6=814 - 6 = 8 neutrons. Carbon-12 has 6 neutrons. Carbon-14 is radioactive, which is why scientists use it to date old organic material.

Bonding depends on valence electrons, the electrons in the outermost shell. Carbon has 4 valence electrons, so it forms 4 covalent bonds. This lets carbon build the chains and rings found in biological molecules.

In a covalent bond, atoms share electrons. If the atoms pull equally, as in O2O_2, the bond is nonpolar. C-H bonds in fats are also usually treated as nonpolar because the difference in electron attraction is small. If one atom is more electronegative, the sharing is unequal and the bond is polar. The oxygen in water is an example. An ionic bond is an attraction between oppositely charged ions. Sodium can transfer an electron to chlorine, forming Na+Na^+ and Cl−Cl^-, which attract each other in table salt.

Hydrogen bonds work differently. They are attractions between molecules, or between distant parts of one large molecule. They do not hold the hydrogen and oxygen atoms together within a water molecule. Because hydrogen bonds are much weaker than covalent bonds, DNA's two strands can unzip while each strand stays intact.

  • Isotope: A form of an element with a particular number of neutrons. Carbon-12 and carbon-14 are isotopes of carbon.
  • Valence electrons: The outer-shell electrons that determine how many bonds an atom forms.
  • Electronegativity: How strongly an atom pulls shared electrons toward itself, with oxygen and nitrogen pulling hard.
  • Ion: An atom that has gained or lost electrons and now carries a charge, like Na+Na^+.

Check yourself: Nitrogen has 7 protons. How many neutrons are in nitrogen-15? (Answer: 8, because 15 - 7 = 8.)

Bond typeWhat happens to electronsRelative strengthBiology example
Nonpolar covalentShared equallyStrongC-H bonds in fatty acid tails
Polar covalentShared unequallyStrongO-H bonds inside a water molecule
IonicTransferred, so opposite ions attractStrong when dry, weaker in waterAttraction between Na+ and Cl- in solid NaCl
Hydrogen bondPartial charges attract between moleculesWeakBetween water molecules; between DNA base pairs
2.3

Organic Compounds: Carbohydrates, Lipids, Proteins, and Nucleic Acids

Cells build polymers by linking monomers. Dehydration synthesis joins two monomers by removing a water molecule. Hydrolysis reverses this by adding water to split the bond, which is what happens during digestion.

There are four macromolecule groups.

  • Carbohydrates are made of C, H, and O in about a 1:2:1 ratio. They supply quick energy (glucose) and structure (cellulose in plant cell walls).
  • Lipids aren't true polymers. Fats are hydrophobic and store about 9 kcal/g, compared with about 4 kcal/g for carbohydrates and proteins. Phospholipids have hydrophilic heads and hydrophobic tails and form cell membranes.
  • Proteins are chains built from 20 kinds of amino acids joined by peptide bonds. Their folded shapes let them work as enzymes, channels, antibodies, and fibers.
  • Nucleic acids (DNA and RNA) are chains of nucleotides that store and pass on genetic information.

Saturated fatty acid tails have only single C-C bonds and can pack tightly. Cis double bonds in unsaturated tails create kinks that make tight packing harder. Fats rich in saturated fatty acids, like butter, are often solid at room temperature, while oils rich in cis unsaturated fatty acids, like olive oil, are often liquid.

Worked example. Two glucose molecules (C6H12O6C_6H_{12}O_6 each) join to make maltose. What is maltose's formula? Adding the atoms gives C12H24O12C_{12}H_{24}O_{12}. Dehydration synthesis removes one H2OH_2O, which leaves C12H22O11C_{12}H_{22}O_{11}. The same logic scales up. A linear protein of 100 amino acids has 99 peptide bonds. In the dehydration synthesis model, forming those bonds would release 99 water molecules. Protein synthesis in a cell uses activated amino acids and does not directly release one water molecule per peptide bond.

  • Dehydration synthesis: A reaction that joins two monomers by removing a water molecule.
  • Hydrolysis: A reaction that breaks a bond between monomers by adding a water molecule.
  • Peptide bond: The covalent bond that links one amino acid to the next in a protein.
  • Phospholipid: A lipid with a hydrophilic phosphate head and two hydrophobic tails that forms the bilayer of cell membranes.

Check yourself: A polysaccharide contains 50 glucose units. How many water molecules are released when it is built, and how many are needed to break it down completely? (Answer: 49 in each case, because 50 monomers are joined by 49 bonds.)

MacromoleculeBuilding blockMain jobsExamples
CarbohydratesMonosaccharidesQuick energy, structureGlucose, starch, glycogen, cellulose
LipidsVaries by lipid; fats contain glycerol and fatty acidsLong-term energy, membranes, hormonesTriglycerides, phospholipids, cholesterol
ProteinsAmino acidsEnzymes, transport, structure, defenseAmylase, hemoglobin, collagen
Nucleic acidsNucleotidesStore and transmit genetic informationDNA, RNA
2.4

Enzymes and Biochemical Reactions

Enzymes are biological catalysts, almost always proteins, that speed up reactions without being used up. They lower activation energy, the energy hill reactants must climb before a reaction can start. They do not change the overall free-energy difference or the equilibrium of the reaction they catalyze.

Each enzyme has an active site whose shape and charges match a specific substrate. In the induced fit model, the active site shifts slightly as the substrate binds. Together they form an enzyme-substrate complex that holds the substrate in position so the reaction happens. The products then leave, and the enzyme binds another substrate. Amylase in your saliva, for example, breaks starch into maltose over and over.

An enzyme's activity depends on its shape and on conditions such as temperature, pH, and substrate concentration. Many human enzymes function well near body temperature, about 37°C. Pepsin in the stomach works best near pH 2, while many other enzymes prefer pH 7 to 8. Too much heat or an extreme pH can disrupt interactions that maintain a protein's fold and denature the enzyme. As substrate concentration increases, the reaction rate approaches a maximum as active sites become saturated.

A competitive inhibitor binds at the active site, and extra substrate can reduce its effect by competing for that site. A noncompetitive inhibitor binds elsewhere and reduces enzyme activity. Adding more substrate does not restore the original maximum rate.

  • Activation energy: The minimum energy reactants need for a reaction to start, which enzymes lower.
  • Active site: The pocket on an enzyme where the substrate binds and the reaction happens.
  • Denaturation: A disruption of a protein's 3D shape, often caused by heat or extreme pH, that can reduce or stop its function.
  • Cofactor: A helper that some enzymes need to function, either a metal ion like Mg2+Mg^{2+} or an organic coenzyme often made from a vitamin.

Check yourself: An enzyme's activity drops sharply when its solution is heated from 37°C to 60°C, and cooling it back down doesn't restore activity. What happened? (Answer: The heat likely denatured the enzyme, disrupting interactions that maintain its 3D shape. The altered enzyme no longer works as well, and cooling did not restore its activity.)

Key terms

TermDefinition
Polar moleculeA molecule with partial positive and partial negative regions because its charge is unevenly distributed. Water is polar because its bonds are polar and its shape is bent.
Covalent bondA bond in which two atoms share one or more pairs of electrons.
Ionic bondAn attraction between oppositely charged ions that forms after one atom transfers electrons to another.
HydrophobicDescribes nonpolar substances, like oils, that don't dissolve in water.
MonomerA small molecule that links with others like it to build a polymer, such as an amino acid or glucose.
PolymerA large molecule made of many repeating monomers joined by covalent bonds.
MacromoleculeA very large molecule, such as a protein, nucleic acid, or polysaccharide. Biology courses also group lipids with these molecules, although not all lipids are large.
EnzymeA biological catalyst that speeds up a reaction by lowering its activation energy. Most enzymes are proteins, but some are RNA molecules.
SubstrateThe specific molecule an enzyme binds and acts on at its active site.

Mistakes to avoid in Biochemistry - The Chemistry of Life

Thinking hydrogen bonds hold the atoms of a water molecule together

The bonds inside one water molecule are polar covalent bonds. Hydrogen bonds are the weaker attractions between separate water molecules. The two names sound alike, which causes the mix-up. When water boils, hydrogen bonds break, but each molecule stays H2O.

Mixing up dehydration synthesis and hydrolysis

Both reactions involve water, so they're easy to swap. Use the word parts to tell them apart. Hydrolysis uses water to split a bond, so water is added to break a polymer apart. Dehydration means water is removed, which happens when a bond is built.

Saying enzymes get used up or make a reaction release more energy

Enzymes are catalysts, so they come out of each reaction unchanged and can be reused thousands of times. They only lower the activation energy hill. The starting and ending energy of the reaction stay the same. On an energy diagram, only the peak gets shorter.

Assuming hotter always means a faster enzyme

Raising temperature can speed an enzyme-catalyzed reaction, but excessive heat can denature the enzyme and reduce the rate. Activity graphs often show a peak across a wide range of temperatures or pH values. A graph may keep rising within the tested range if that range does not reach the optimum.

Study unit 2 other ways

Ready to review Unit 2?Start with the notes, check the topic cards, and use the practice or resource links when they are available for this course.