Untitled Quiz

Biomolecules

• Biomolecules are carbon-containing compounds found in living organisms
• Divided into inorganic (water, minerals, CO₂) and organic (carbohydrates, lipids, nucleic acids)
• Chemical analysis of living tissue involves grinding, filtering, and separating components into filtrate (acid-soluble) and residue (acid-insoluble) fractions

How to Analyze Chemical Composition of Living Tissue

• Grind the tissue to obtain a slurry.
• Filter the slurry through cheesecloth or cotton.
• Separate the filtrate and residue.
• Filtrate contains low-molecular-weight molecules (18-800 Daltons), including proteins, peptides, and sugars.
• Residue contains high-molecular-weight molecules (above 10,000 Daltons), including proteins, nucleic acids, polysaccharides, and lipids.

Types of Biomolecules based on Molecular Weight

• Micromolecules: Low molecular weight (less than 1000 Daltons), found in filtrate. Include amino acids, nucleotides, monosaccharides, and fatty acids.
• Macromolecules: High molecular weight (above 1000 Daltons), found in residue. Include carbohydrates, proteins, nucleic acids, and lipids

Metabolites

• Metabolites are biomolecules involved in metabolic reactions.
• Primary metabolites: Have identifiable functions in normal body processes (e.g., amino acids, proteins, nucleic acids).
• Secondary metabolites: Not directly involved in primary body functions, but can have roles in plant development, defense, or signaling (e.g., alkaloids, terpenoids, pigments).

Experiment to Prove Inorganic Elements in Living Cells

• Take a sample of living tissue (like a leaf).
• Dry the tissue sample.
• Burn the tissue (heat it until all water evaporates).
• The residue is the ash, which contains inorganic elements.

Amino Acids

• Amino acids are organic compounds containing an amino group (-NH₂) and a carboxyl group (-COOH).
• Twenty different amino acid types exist, each distinguished by the R group or side chain.
• Classified based on properties of R-group (basic, acidic, polar, nonpolar).
• 10 essential amino acids are not produced by the body and must be obtained through diet.

Properties of Amino Acids

• Amphoteric properties: Can act as either an acid or a base.
• Zwitterion formation: Can exist as dipolar ions (ionized form)

Types of Proteins

• Proteins are polymers of amino acids linked by peptide bonds.
• Primary structure: Linear sequence of amino acids.
• Secondary structure: Local folding of the polypeptide chain (alpha helix or beta sheet), stabilized by hydrogen bonds.
• Tertiary structure: 3D arrangement of the polypeptide chain, stabilized by various interactions (hydrogen bonds, disulfide bonds, hydrophobic interactions).
• Quaternary structure: Arrangement of multiple polypeptide chains in a protein.

Carbohydrates

• Carbohydrates are organic compounds composed of carbon, hydrogen, and oxygen with a general formula (CH₂O)ₙ.
• Classified into monosaccharides (single units), oligosaccharides (short chains), and polysaccharides (long chains).
• Monosaccharides: Simple sugars like glucose, fructose, and galactose.
• Oligosaccharides: Short chains of monosaccharides linked by glycosidic bonds(e.g., sucrose, lactose, maltose).
• Polysaccharides: Long chains of monosaccharides (e.g., starch, cellulose, glycogen).

Monosaccharides

• Have general formula (CH₂O)ₙ where n ranges from 3 to 7.
• Can be straight chain or ring structures.
• Examples include glucose, fructose, and ribose.

Oligosaccharides

• Formed by linking 2-8 monosaccharides.
• Examples include sucrose, lactose, and maltose.

Polysaccharides

• Formed by linking many monosaccharides via glycosidic bonds.
• Examples include starch, cellulose, and glycogen.

Nucleic Acids

• Nucleic acids are polymers of nucleotides, which are composed of a nitrogenous base, a pentose sugar, and a phosphate group.
• Two types exist: DNA and RNA.
• Structure includes: Pentose Sugar, N-base, PO₄.

Lipids

• Lipids are a diverse group of hydrophobic molecules, insoluble in water.
• Classified into simple lipids, conjugated lipids, and derived lipids.
• Simple lipids: Made up only of fatty acids and alcohol (e.g., triglycerides).
• Conjugated lipids: Contain additional groups like phosphate or carbohydrates (e.g. phospholipids, glycolipids).
• Derived lipids: Derived from other lipids (e.g., cholesterol, steroids).

Enzymes

• Enzymes are biological catalysts that accelerate chemical reactions in living organisms.
• Composed primarily of proteins (many are composed of protein as well as cofactors).
• Enzymes have specific active sites where substrates bind and reactions occur.
• Enzymes are essential for all the metabolic processes in a living organisms.
• Different factors, including temperature, pH, and substrate concentration, affect enzyme activity.

Rate of Reaction

• The rate of reaction is the speed at which products are formed or reactants are consumed per unit of time.
• Enzymes accelerate reactions by lowering the activation energy, the energy required for a reaction to proceed.
• The rate of reaction is affected by factors like temperature, pH, substrate concentration, and enzyme concentration.

Catalyzed Reaction

• Reaction where rate is enhanced by enzymes.
• Enzymes reduce the activation energy to enable a faster rate of reaction.

Enzyme Inhibition

• Enjyme inhibition is the decrease in the rate of catalysis by an enzyme as a result of the presence of an inhibitor.
• Competitive inhibition: Inhibitor competes with the substrate for the active site of the enzyme.
• Non-competitive inhibition: Inhibitor binds to a site other than the active site, changing the enzyme's conformation and reducing its activity.

Classification of Enzymes

• Oxidoreductases: Catalyze oxidation-reduction reactions.
• Transferases: Catalyze the transfer of a group from one molecule to another.
• Hydrolases: Catalyze the hydrolysis of a substrate.
• Lyases: Catalyze the breakage of a substrate.
• Isomerases: Catalyze the isomerization of a substrate.
• Ligases: Catalyze the joining of two molecules.

Co-factors

• Non-protein components that bind to enzymes to assist in catalysis.
• Prosthetic groups: Tightly bound, organic molecules.
• Co-enzymes: Loosely bound, organic molecules (e.g., vitamins).
• Metal ions: Inorganic ions (e.g., zinc, magnesium).