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General 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.

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