BackGeneral Chemistry Study Guide: Intermolecular Forces, Solution Chemistry, Acids & Bases, and Biochemistry Fundamentals
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Chapter 7: Attractive Forces & Lipids
Intermolecular Attractions & Strength
Intermolecular forces are the forces of attraction between molecules, which determine many physical properties of substances, such as boiling and melting points.
London Dispersion Forces: Weakest, present in all molecules, especially nonpolar ones.
Dipole-Dipole Interactions: Occur between polar molecules.
Hydrogen Bonding: Strongest type, occurs when H is bonded to N, O, or F.
Example: Water exhibits hydrogen bonding, leading to its high boiling point compared to other group 16 hydrides.
Gases & Liquid-Gas Laws
Gas laws describe the relationships between pressure, volume, temperature, and amount of gas.
Boyle's Law: (at constant T and n)
Charles's Law: (at constant P and n)
Ideal Gas Law:
Example: Calculating the volume of a gas at different temperatures using Charles's Law.
Phase Changes & Diagrams
Phase changes are transitions between solid, liquid, and gas states. Phase diagrams show the conditions under which these phases exist.
Melting, Freezing, Vaporization, Condensation, Sublimation, Deposition
Triple Point: All three phases coexist.
Lipid Characteristics
Lipids are a diverse group of hydrophobic biomolecules, including fats, oils, and steroids.
Types: Fatty acids, triglycerides, phospholipids, steroids.
Solubility: Generally insoluble in water, soluble in nonpolar solvents.
Membrane Lipids & the Bilayer
Phospholipids form the basic structure of cell membranes, creating a bilayer that separates the cell from its environment.
Hydrophilic heads face outward; hydrophobic tails face inward.
Chapter 8: Solution Chemistry
Factors Affecting Solubility
Solubility depends on the nature of solute and solvent, temperature, and pressure (for gases).
"Like dissolves like": Polar solutes dissolve in polar solvents; nonpolar in nonpolar.
Temperature: Solubility of solids increases with temperature; gases decrease.
Electrolytes & Nonelectrolytes
Electrolytes dissociate into ions in solution and conduct electricity; nonelectrolytes do not.
Strong electrolytes: Completely dissociate (e.g., NaCl).
Weak electrolytes: Partially dissociate (e.g., acetic acid).
Nonelectrolytes: Do not dissociate (e.g., sugar).
Solution Calculations
Concentration expresses the amount of solute in a given amount of solution.
Molarity (M):
Percent by mass/volume:
Diffusion & Cellular Transport
Diffusion is the movement of particles from high to low concentration. In biology, this includes osmosis (water movement) and facilitated diffusion (via proteins).
Osmosis: Water moves across a semipermeable membrane toward higher solute concentration.
Active transport: Movement against a concentration gradient, requiring energy.
Chapter 9: Acids, Bases, Equilibrium & Buffers
Acids & Bases (Brønsted-Lowry)
Acids donate protons (H+); bases accept protons.
Strong acids/bases: Completely ionize in water.
Weak acids/bases: Partially ionize.
Ionization & Neutralization
Ionization is the process of forming ions in solution. Neutralization is the reaction of an acid with a base to form water and a salt.
General equation:
Chemical Equilibrium
At equilibrium, the rates of the forward and reverse reactions are equal.
Equilibrium constant: (at equilibrium)
Le Châtelier's Principle
If a system at equilibrium is disturbed, it will shift to counteract the disturbance.
Changes in concentration, temperature, or pressure can shift equilibrium position.
pH, pOH, and Buffer Systems
pH measures the acidity of a solution; buffers resist changes in pH.
pH:
pOH:
Relationship: (at 25°C)
Buffer: Solution of weak acid and its conjugate base (or vice versa).
Henderson-Hasselbalch Equation:
Chapter 10: Amino Acids, Proteins & Enzymes
Amino Acids: Structure & Properties
Amino acids are the building blocks of proteins, each containing an amino group, carboxyl group, hydrogen, and unique side chain (R group).
Classification: Polar, nonpolar, acidic, basic, aromatic, etc.
Protein Structure & Terminology
Proteins have four levels of structure:
Primary: Sequence of amino acids.
Secondary: Local folding (α-helix, β-sheet).
Tertiary: 3D folding of a single polypeptide.
Quaternary: Association of multiple polypeptides.
Enzymes: Function & Mechanism
Enzymes are biological catalysts that speed up chemical reactions by lowering activation energy.
Active site: Region where substrate binds.
Specificity: Enzymes are specific to substrates.
Factors affecting activity: pH, temperature, inhibitors.
Enzyme Inhibition
Enzyme activity can be regulated by inhibitors.
Competitive inhibitors: Bind to active site.
Noncompetitive inhibitors: Bind elsewhere, changing enzyme shape.