Biological molecules

Triglycerides and Phospholipids

  • Formation: Both triglycerides and phospholipids are formed through a condensation reaction involving glycerol and fatty acids.

    • Triglycerides: One glycerol molecule combines with three fatty acids.

    • Phospholipids: One glycerol molecule combines with two fatty acids and a phosphate group.

Properties of Triglycerides

  1. Energy Storage: Have a high ratio of carbon-hydrogen bonds compared to carbon atoms, making them an efficient form of energy storage.

  2. Metabolic Water Source: Upon oxidation, triglycerides can release water, which is essential for organisms like camels.

  3. Hydrophobic Nature: Their large size and hydrophobic characteristics make them insoluble in water, thus not affecting osmotic processes.

  4. Low Mass: They can be stored without substantial increase in mass.

Fatty Acids

  • Saturated Fatty Acids: Contain only single bonds between carbon atoms, making them saturated with hydrogen.

  • Unsaturated Fatty Acids: Include at least one double bond between carbon atoms, creating kinks that cause lower density and fluidity in lipids.

Phospholipid Structure

  • Comprises two fatty acids, glycerol, and a phosphate group, leading to unique properties that involve hydrophilic (water-attracting) and hydrophobic (water-repelling) regions.

Proteins

Building Blocks

  • Amino Acids: The monomers of proteins, consisting of an amino group and a carboxyl group.

  • Dipeptides & Polypeptides: Formed by the condensation reaction of two amino acids or many amino acids, respectively.

Structures of Proteins

  1. Primary Structure: Sequence of amino acids in a polypeptide chain.

  2. Secondary Structure: Folding of the polypeptide chain into structures such as alpha-helices or beta-pleated sheets, stabilized by hydrogen bonds.

  3. Tertiary Structure: Further folding leads to a unique three-dimensional shape of the protein, maintained by various bonds including ionic and disulfide bonds.

  4. Quaternary Structure: Involves two or more polypeptide chains forming a functional protein.

Enzymes

  • Enzymes are typically tertiary structured proteins that lower the activation energy of reactions they catalyze.

  • Active Site: Specific region of the enzyme that binds to substrates due to its unique shape determined by the protein's tertiary structure.

Models of Enzyme Action

  • Lock and Key Model: Earlier concept of enzyme-substrate interactions.

  • Induced Fit Model: Active site changes shape to fit the substrate upon binding, enhancing the reaction.

Factors Affecting Enzyme Activity

  • Temperature: Optimal temperatures enhance enzyme activity, but extremes can denature enzymes.

  • pH: Varies by enzyme; inappropriate levels can disrupt the ionic and hydrogen bonds stabilizing the tertiary structure.

  • Substrate Concentration: Insufficient substrate slows reactions, but saturating substrates lead to maximum enzyme activity.

Enzyme Inhibitors

  1. Competitive Inhibitors: Similar shape to substrates, competing for the active site, can be outcompeted by higher substrate concentrations.

  2. Non-Competitive Inhibitors: Bind to an allosteric site, changing the shape of the active site, preventing substrate binding regardless of concentration.

Chemical Tests for Biomolecules

  • Starch: Test with iodine; positive result shows blue-black coloration.

  • Reducing Sugars: Test with Benedict's solution; positive results range from green to brick red based on concentration.

  • Non-Reducing Sugars: Require acid hydrolysis prior to Benedict’s test.

  • Proteins: Biuret test gives purple coloration for positive.

  • Lipids: Dissolve in ethanol, then add distilled water; positive indicates white emulsion.

DNA (Deoxyribonucleic Acid)

  • Structure: Double helix formed by nucleotides (deoxyribose sugar, a phosphate group, and nitrogenous bases).

  • Nucleotides: Join through phosphodiester bonds to form polynucleotides.

  • Base Pairing: Adenine pairs with thymine, cytosine pairs with guanine.

RNA (Ribonucleic Acid)

  • Composition: Single-stranded polymer of nucleotides with ribose sugar and uracil base instead of thymine.

  • Function: Transfers genetic code from DNA to ribosomes.

DNA Replication

  1. Separation of Strands: Parental strands unwind.

  2. Base Pairing: Free nucleotides pair with complementary bases of the template strand.

  3. Formation of Daughter DNA: Nucleotides bond through condensation reactions with the help of DNA polymerase.

ATP (Adenosine Triphosphate)

  • Function: Primary energy carrier in cells; releases energy during hydrolysis.

  • Energy Transfer: Phosphate group from ATP can be transferred to other molecules, increasing their reactivity.

Water Properties and Inorg. Ions

  1. Metabolite: Integral in biochemical reactions.

  2. Solvent: High capacity for solvation in reactions.

  3. High Heat Capacity: Regulates temperature.

  4. Cohesion: High surface tension due to strong molecular interactions.

  5. Ions in Physiology: Various inorganic ions serve roles in biological processes.

    • Hydrogen Ions: Influence pH and enzyme function.

    • Iron Ions: Critical for oxygen transport in hemoglobin.

    • Sodium Ions: Play a role in sodium-glucose co-transport mechanisms.

    • Phosphate Ions: Essential components of ATP and DNA structural integrity.