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02.01 Biochemistry Principals

1. Basic Chemical Concepts

Atoms and Elements

  • Atoms: The fundamental units of matter, consisting of protons, neutrons, and electrons.
  • Elements: Pure substances composed of only one type of atom, each defined by its atomic number (number of protons).

Elements tend to fill their outermost shells with electrons. To do this, they can either donate or accept electrons from other elements.

Molecules and Compounds

  • Molecules: Two or more atoms bonded together, representing the smallest unit of a chemical compound that retains its properties.
  • Compounds: Substances formed when two or more different elements combine chemically in fixed proportions (e.g., water, CO₂).

In the formation of an ionic compound, metals lose electrons and nonmetals gain electrons to achieve an octet.

Chemical Bonds

  • Ionic Bonds: Formed when electrons are transferred from one atom to another, resulting in oppositely charged ions that attract each other.
  • Covalent Bonds: Involve the sharing of electron pairs between atoms, creating a strong bond.
  • Hydrogen Bonds: Weak bonds between a hydrogen atom and a highly electronegative atom (such as oxygen or nitrogen) in another molecule.
  • Van der Waals Forces: Weak, non-specific interactions caused by temporary dipoles in molecules.

he water molecule (left) depicts a polar bond with a slightly positive charge on the hydrogen atoms and a slightly negative charge on the oxygen. Examples of nonpolar bonds include methane (middle) and oxygen (right).

2. Organic Chemistry

Role of Carbon

  • Carbon’s Versatility: Carbon has four valency electrons, allowing it to form four covalent bonds with other atoms, including other carbon atoms. This property enables the formation of complex and diverse organic molecules.
  • Catenation: The ability of carbon to form long chains and rings, providing a backbone for complex structures.

Hydrophobic and Hydrophilic Interactions

  • Hydrophobic: Molecules or regions of molecules that repel water, typically nonpolar substances (e.g., lipid tails in phospholipids).
  • Hydrophilic: Molecules or regions that attract water, typically polar or charged substances (e.g., hydroxyl groups in sugars).

Monomers and Polymers

  • Monomers: Small, simple molecules that can join together to form larger, more complex molecules.
    • Examples: Glucose (monomer of carbohydrates), amino acids (monomers of proteins), nucleotides (monomers of nucleic acids), fatty acids and glycerol (components of lipids).
  • Polymers: Large, complex molecules made up of repeating monomer units.
    • Examples:
      • Carbohydrates: Polysaccharides like starch and cellulose.
      • Proteins: Polymers of amino acids.
      • Nucleic Acids: DNA and RNA, polymers of nucleotides.
      • Lipids: While not always true polymers, they are composed of fatty acid chains and glycerol.

Functional Groups

  • Hydroxyl (-OH): Found in alcohols and carbohydrates.
  • Carbonyl (C=O): Present in ketones and aldehydes.
  • Amino (-NH₂): Found in amino acids.
  • Phosphate (-PO₄³⁻): Present in nucleotides and ATP.
  • Carboxyl (-COOH): Found in fatty acids and amino acids.

Isomerism

  • Structural Isomers: Compounds with the same molecular formula but different bonding arrangements.
  • Stereoisomers: Compounds with the same molecular formula and bonding but different spatial arrangements.

Structural Isomers

3. Metabolism

Catabolism and Anabolism

  • Catabolism: Metabolic pathways that break down complex molecules into simpler ones, releasing energy.
    • Examples: Glycolysis, the citric acid cycle, and fatty acid oxidation.
    • Products: ATP, NADH, and other energy carriers.
  • Anabolism: Metabolic pathways that build complex molecules from simpler ones, requiring energy.
    • Examples: Protein synthesis, DNA replication, and gluconeogenesis.
    • Products: Proteins, nucleic acids, and complex carbohydrates.

Enzymes

  • Function: Biological catalysts that speed up chemical reactions by lowering the activation energy.
  • Enzyme Kinetics: Study of the rates of enzyme-catalyzed reactions.
  • Regulation: Enzyme activity can be controlled by inhibitors, activators, and feedback mechanisms.

4. Energy Transfer and Thermodynamics

ATP (Adenosine Triphosphate)

  • Role: The primary energy carrier in cells.
  • ATP Hydrolysis: The reaction ATP → ADP + Pi releases energy used for cellular processes.

Redox Reactions

  • Oxidation: Loss of electrons.
  • Reduction: Gain of electrons.
  • Electron Transport Chain: Series of redox reactions in cellular respiration that generate ATP.

Thermodynamics

  • Enthalpy (ΔH): Total heat content of a system.
  • Entropy (ΔS): Measure of disorder or randomness in a system.
  • Gibbs Free Energy (ΔG): Determines the spontaneity of a reaction (ΔG = ΔH – TΔS). Negative ΔG indicates a spontaneous reaction.

5. pH and Buffer Systems

pH Scale

  • Range: 0-14, measuring the acidity or basicity of a solution.
    • Acid: pH < 7
    • Base: pH > 7
    • Neutral: pH = 7

Buffers

  • Function: Solutions that resist changes in pH by neutralizing added acids or bases.
  • Biological Importance: Maintain the optimal pH for enzymatic activities and cellular functions.

6. Properties of Water

Polarity

  • Structure: Water molecules have a partial positive charge on hydrogen atoms and a partial negative charge on the oxygen atom.
  • Hydrogen Bonding: Polar nature allows water to form hydrogen bonds, contributing to its unique properties.

Cohesion and Adhesion

  • Cohesion: Attraction between water molecules, leading to surface tension.
  • Adhesion: Attraction between water molecules and other substances, aiding in processes like capillary action.

High Specific Heat

  • Definition: Ability of water to absorb or release large amounts of heat with minimal temperature change.
  • Biological Significance: Helps regulate temperature in organisms and environments.

Solvent Properties

  • Universal Solvent: Dissolves many substances, facilitating biochemical reactions and nutrient transport.
  • Hydrophilic and Hydrophobic Interactions: Determines solubility and interactions of molecules in aqueous environments.

7. Additional Key Concepts

Chemical Equilibrium

  • Definition: A state where the rate of the forward reaction equals the rate of the reverse reaction.
  • Biological Relevance: Many biochemical reactions are reversible and exist in equilibrium.
    • Le Chatelier’s Principle: If a dynamic equilibrium is disturbed by changing the conditions, the position of equilibrium moves to counteract the change.
    • Examples in Biology: Binding of oxygen to hemoglobin, enzyme-substrate interactions.

Acid-Base Chemistry

  • Importance: Critical for enzyme function, metabolic pathways, and maintaining cellular pH.
  • Buffers: Systems that maintain acid-base balance in biological fluids.
    • Buffer Systems in the Body: Bicarbonate buffer system, phosphate buffer system, protein buffers.
  • pKa: The pH at which half of the buffer’s species are deprotonated, important for understanding buffer capacity.

Isotopes and Atomic Mass

  • Mass Spectrometry: Technique used to determine the composition of isotopes in molecules, aiding in metabolic studies.
  • Isotopes: Atoms of the same element with different numbers of neutrons.
  • Stable vs. Radioactive Isotopes: Stability affects their roles in biological systems and tracing mechanisms.
  • Atomic Mass: Weighted average mass of an element’s isotopes, important in biochemical calculations and tracing metabolic pathways.

Practise Questions

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