Quiz Review
Chapter 2: Atoms & Chemical Bonds
1. Elements, Atoms, Molecules, and Compounds
Element: A substance that cannot be broken down into simpler substances by chemical reactions.
Atom: The smallest unit of matter that retains all properties of an element.
Molecule: Two or more atoms held together by covalent bonds.
Compound: Two or more different elements combined in a fixed ratio.
A molecule containing different elements is also considered a compound.
2. Atomic Structure & Subatomic Particles
Subatomic Particles:
Protons: Positive charge ().
Neutrons: Neutral / no charge ().
Electrons: Negative charge (); determine an atom's overall charge and chemical reactivity.
Atomic Calculations:
3. Isotopes
Isotopes: Atoms of the same element that have the same number of protons but different numbers of neutrons.
Radioactive Isotopes: Unstable isotopes whose nuclei decay spontaneously, releasing particles and energy. Used as biological tracers to track metabolic pathways and biological processes.
4. Electrons & Valence Shells
Electrons reside in energy levels or electron shells surrounding the nucleus.
Electrons farther from the nucleus possess higher potential energy.
Valence Shell: The outermost electron shell.
Valence Electrons: Electrons in the valence shell available for chemical bonding.
Atom reactivity is driven by filling or completing its valence shell.
5. Chemical Bonds & Interactions
Covalent Bonds: Sharing of a pair of valence electrons by two atoms.
Single Bond: Sharing pair of electrons.
Double Bond: Sharing pairs of electrons.
Bonding capacity depends on the number of unpaired valence electrons.
Electronegativity: An atom's attraction for shared electrons in a covalent bond.
Nonpolar Covalent Bond: Electrons are shared equally (or nearly equally) due to similar electronegativity.
Polar Covalent Bond: Electrons are shared unequally due to differing electronegativity.
Example in : Oxygen is more electronegative than hydrogen, pulling shared electrons closer to form a partial negative charge () on oxygen and partial positive charges () on hydrogen.
Electronegativity Difference & Bond Types
: Nonpolar Covalent (shared equally, no charges)
: Polar Covalent (shared unequally, partial charges , )
: Ionic (electrons transferred completely, full charges , )
Ionic Bonds: Complete transfer of electrons from one atom to another, resulting in oppositely charged ions that attract each other.
Cation: A positively charged ion formed by losing electrons (e.g., ).
Anion: A negatively charged ion formed by gaining electrons (e.g., ).
Example: formation where loses electron () and gains electron ().
Hydrogen Bonds: Noncovalent attraction between a hydrogen atom covalently bonded to an electronegative atom and another electronegative atom.
Van der Waals Interactions: Weak, transient attractions between adjacent molecules caused by temporary local partial charges.
Example: Enables geckos to climb vertical surfaces.
Shape & Function: Molecular structure dictates biological activity, essential for signal recognition, enzymes, and cell receptors.
Chapter 3: Water & the Fitness of the Environment
1. Water & Polarity
Water () is a polar molecule held together internally by polar covalent bonds between oxygen and hydrogen.
Hydrogen bonds continuously form and break between adjacent water molecules.
2. Four Emergent Properties of Water
Cohesion & Adhesion:
Cohesion: Attraction between identical water molecules via hydrogen bonding.
Adhesion: Attraction between water molecules and other polar or charged substances.
Surface Tension: Measure of how difficult it is to stretch or break the surface of a liquid.
Enables water transport against gravity in plants.
Expansion Upon Freezing:
Water expands as it freezes because hydrogen bonds stabilize into a crystalline lattice structure, keeping ice molecules farther apart than in liquid water.
Ice is less dense than liquid water and floats, insulating aquatic environments below.
Versatility as a Solvent:
Water is an effective solvent due to its polarity.
Hydration Shell: A sphere of water molecules surrounding dissolved ions ( oxygen attracts ; hydrogen attracts ).
Hydrophilic: Substances with an affinity for water (polar or ionic).
Hydrophobic: Substances that repel water (nonpolar or nonionic).
Temperature Moderation:
Kinetic Energy: Energy of motion; average kinetic energy is measured as temperature.
Thermal Energy: Total kinetic energy of molecules in a body of matter.
High Specific Heat: Water absorbs or releases large amounts of heat with minimal temperature change.
Evaporative Cooling: As liquid evaporates, high-energy molecules escape, cooling the remaining surface.
Chapter 4: Carbon & Molecular Diversity
1. Importance of Carbon
Carbon forms organic compounds by forming up to covalent bonds with elements such as hydrogen, oxygen, nitrogen, and other carbon atoms.
2. Carbon Skeletons & Hydrocarbons
Carbon chains form skeletons that vary in length, branching, double bond position, and rings.
Hydrocarbons: Organic molecules consisting solely of carbon and hydrogen (e.g., nonpolar regions of lipids) that store large amounts of energy.
3. Isomers
Isomer: Compounds with identical molecular formulas but distinct structural arrangements and properties.
Structural Isomers: Differ in the covalent arrangement of their atoms.
Cis-Trans Isomers: Differ in spatial arrangements around a rigid double bond.
4. Functional Groups
Specific chemical groups attached to carbon skeletons that participate in chemical reactions or modify molecular function.
Example Steroids (Estradiol vs. Testosterone):
Both share the same four-ring carbon skeleton structure.
Estradiol: Features a hydroxyl group ().
Testosterone: Features a carbonyl group () and a methyl group ().
Differences in functional groups lead to binding with different cellular receptors.
5. ATP (Adenosine Triphosphate)
Primary energy-transferring molecule in cells consisting of adenosine attached to three phosphate groups.
Reaction for energy release:
Chapter 5: Macromolecules
1. Proteins
Building Blocks: Amino acids linked by peptide bonds to form polypeptide chains.
Amino Acid Structure: Central carbon (alpha-carbon), amino group (), carboxyl group (), hydrogen atom, and a variable R group (side chain).
Nonpolar R groups = Hydrophobic (positioned in protein interior).
Polar / Charged R groups = Hydrophilic (positioned on protein exterior).
Four Levels of Protein Structure:
Primary Structure: Linear sequence of amino acids.
Secondary Structure: Coils (alpha-helices) and folds (beta-pleated sheets) held by hydrogen bonds along the polypeptide backbone.
Tertiary Structure: Overall 3D shape resulting from interactions among R group side chains.
Quaternary Structure: Association of two or more individual polypeptide chains working together.
Denaturation: Loss of a protein's native 3D structure and function due to changes in temperature, pH, or salt concentration.
Structural variation example: A single amino acid change in hemoglobin causes sickle-cell anemia.
2. Nucleic Acids
Function: Store, transmit, and express hereditary information (DNA and RNA).
Building Blocks: Nucleotides linked in a direction.
Nucleotide Components:
-carbon sugar (deoxyribose or ribose)
Phosphate group
Nitrogenous base
Nitrogenous Bases:
Purines: Adenine () and Guanine () (two rings).
Pyrimidines: Cytosine (), Thymine (), and Uracil () (single ring).
Base Pairing Rules:
(DNA) or (RNA) via hydrogen bonds.
via hydrogen bonds.
3. DNA vs. RNA
Sugar: Deoxyribose in DNA vs. Ribose in RNA.
Bases: Thymine () in DNA vs. Uracil () in RNA.
Structure: DNA is double-stranded (forming a double helix); RNA is single-stranded (can fold into diverse 3D structures).