Document 9

Chapter 2 – The Chemistry of Life

Elements

  • Definition: A substance composed of only one type of atom that cannot be broken down into simpler substances with different properties.

Major Subatomic Particles of an Atom

  • Proton: Positive charge, located in the nucleus.

  • Neutron: No charge (neutral), located in the nucleus.

  • Electron: Negative charge, located in the electron cloud.

  • Atomic Number: The number of protons equals the atomic number.

  • Atomic Mass: Protons and neutrons weigh approximately 1 amu, and the total of protons and neutrons equals the atomic mass.

  • Isotopes: Atoms of the same element that differ in the number of neutrons, resulting in different atomic masses.

Chemical Bonds and Reactions

  • Molecule: Interaction between 2 or more atoms that can be identical (e.g., O2).

  • Compound: Interaction between 2 or more atoms from different elements (e.g., CO2).

  • Cation: Atoms with a positive charge (e.g., Na+).

  • Anion: Atoms with a negative charge (e.g., Cl-).

Page 2 - Types of Bonds

Ionic Bonds

  • Definition: Transferring of electrons from one atom to another. The resulting positive and negative charged ions are attracted to one another.

    • Example: NaCl (Na+ ... Cl-), KCl (K+ ... Cl-).

Covalent Bonds

  • Nonpolar Covalent Bonds: Equal sharing of electrons (e.g., O2, CO2) - strongest bond.

  • Polar Covalent Bonds: Unequal sharing of electrons (e.g., H2O) - second strongest bond.

  • Hydrogen Bonds: Attraction between hydrogen bonded in one molecule and an electronegative atom in another (e.g., adjacent H2O molecules, DNA base pairs) - weakest bond.

Metabolism

  • Definition: The sum of all chemical reactions that occur in the body.

    1. Anabolic Reactions: Endergonic reactions involving synthesis of larger molecules from smaller ones (e.g., combining amino acids to form protein).

    2. Catabolic Reactions: Exergonic reactions involving decomposition of larger molecules into simpler ones (e.g., digestive enzymes breaking down starch).

Page 3 - Properties of Water

  1. Strong Polarity: Water dissolves a wide range of substances due to its polar covalent bonds.

  2. High Heat Capacity: When heat is applied, hydrogen bonds break, absorbing heat energy without significantly increasing temperature.

  3. High Heat of Vaporization: Evaporation of water from skin removes a lot of heat, functioning as a cooling mechanism.

  4. Cohesion: Water molecules cling to one another because of hydrogen bonds, acting as an effective transport medium and lubricant.

Solubility

  • Hydrophilic (e.g., salt) vs. Hydrophobic (e.g., vegetable oils).

  • Electrolytes: Ionic compounds dissociating into cations and anions (e.g., Acids HCl, Bases KOH).

Page 4 - pH Scale

  • Acidity and Basicity:

    • 0 to < 7 is acidic (more H+ than OH-).

    • 7 is neutral (H+ = OH-).

    • 7 to 14 is basic/alkaline (more OH- than H+).

Organic Molecules

Anabolic Reactions (Creating)

  • Dehydration Synthesis: Forming macromolecules (polymers) by joining subunits (monomers) through covalent bonding, usually removing water.

Catabolic Reactions (Decomposing)

  • Hydrolysis: Breaking down macromolecules into subunits by adding water.

Building Blocks of Macromolecules

  • Carbohydrates: Monosaccharides (e.g., glucose).

  • Proteins: Amino acids.

  • Lipids: Triglycerides (glycerol + fatty acids).

  • Nucleic Acids: Nucleotides.

Page 5 - Carbohydrates

  • Primary Monosaccharides: Glucose, deoxyribose, galactose, ribose, fructose.

  • Disaccharides: Two monosaccharides combined (e.g., sucrose: glucose + fructose; maltose: glucose + glucose; lactose: glucose + galactose).

  • Molecular Formula: C6H12O6.

  • Glycogen: A polysaccharide composed of glucose monomers.

Page 6 - Proteins

Structure of Proteins

  • Basic Structure: H2N-C-COOH (R group varies)

    • Amino Group: H2N.

    • Carboxyl Group: COOH.

Levels of Protein Structure

  1. Primary Structure: Polypeptide chains.

  2. Secondary Structure: Alpha helix and beta-pleated sheets (stabilized by hydrogen bonds).

  3. Tertiary Structure: 3-D shape of polypeptide; determines function (e.g., globular, fibrous proteins).

  4. Quaternary Structure: More than one polypeptide chain (e.g., hemoglobin).

Denaturation of Proteins

  • Causes: Extreme heat and pH changes can denature proteins, altering their function.

Enzymes

  • Function: Biological catalysts that speed up reactions without being consumed, specific to substrates, lowering activation energy.