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
Energy Storage: Have a high ratio of carbon-hydrogen bonds compared to carbon atoms, making them an efficient form of energy storage.
Metabolic Water Source: Upon oxidation, triglycerides can release water, which is essential for organisms like camels.
Hydrophobic Nature: Their large size and hydrophobic characteristics make them insoluble in water, thus not affecting osmotic processes.
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
Primary Structure: Sequence of amino acids in a polypeptide chain.
Secondary Structure: Folding of the polypeptide chain into structures such as alpha-helices or beta-pleated sheets, stabilized by hydrogen bonds.
Tertiary Structure: Further folding leads to a unique three-dimensional shape of the protein, maintained by various bonds including ionic and disulfide bonds.
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
Competitive Inhibitors: Similar shape to substrates, competing for the active site, can be outcompeted by higher substrate concentrations.
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
Separation of Strands: Parental strands unwind.
Base Pairing: Free nucleotides pair with complementary bases of the template strand.
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
Metabolite: Integral in biochemical reactions.
Solvent: High capacity for solvation in reactions.
High Heat Capacity: Regulates temperature.
Cohesion: High surface tension due to strong molecular interactions.
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.