Biological molecules

Subdecks (2)

Cards (51)

  • Secondary structure involves hydrogen bonds between peptide groups forming alpha helices or beta pleated sheets.
  • Primary structure refers to the sequence of amino acids in a protein chain.
  • The three-dimensional structure of proteins is determined by the primary, secondary, tertiary, and quaternary structures.
  • Tertiary structure is the overall shape of the protein, determined by interactions such as disulfide bridges, ionic bonds, van der Waals forces, and hydrophobic interactions.
  • Tertiary structure is formed by interactions within one polypeptide, such as disulfide bridges, ionic bonds, van der Waals forces, and hydrophobic interactions.
  • Quaternary structure refers to multiple polypeptides coming together to form one functional unit.
  • Quaternary structure refers to multiple polypeptides coming together to form one functional unit.
  • Denaturation can occur due to changes in pH, temperature, or chemical agents that disrupt noncovalent interactions.
  • Denaturation can occur due to changes in pH, temperature, or chemical agents that disrupt noncovalent interactions.
  • Quaternary structure describes how multiple polypeptides interact with each other to form a functional protein complex.
  • Protein folding occurs through interactions such as disulfide bridges, ionic bonds, van der Waals forces, and hydrophobic interactions.
  • Benedict’s solution can be used to test for reducing sugars, including glucose, fructose, and maltose
  • Benedict’s solution does not test for sucrose
  • Acid hydrolysis can break glycosidic bonds in non-reducing sugars
  • Semi-quantitative methods for Benedict’s test:
    • Measure time for color change
    • Use colorimetry to estimate concentration (higher glucose concentration means lower absorbance)
  • Iodine/potassium iodide test turns blue/black if starch is present
  • Emulsion test with ethanol and water shows a milky color for lipids
  • Biuret test changes color from blue to purple in the presence of proteins
  • Carbohydrates consist of monosaccharides, disaccharides, and polysaccharides
  • Monosaccharides like glucose are important substrates for respiration
  • Disaccharides include maltose, sucrose, and lactose
  • Polysaccharides like glycogen, starch, and cellulose are formed by glycosidic bonds
  • Glycogen is the main energy storage molecule in animals, formed by alpha glucose with many side branches
  • Starch consists of amylose and amylopectin, with different structures affecting digestion speed
  • Cellulose provides structural support in plant cells, composed of beta glucose chains
  • Saturated lipids in animal fats lack carbon-carbon double bonds, while unsaturated lipids in plants contain double bonds
  • Triglycerides are composed of glycerol and three fatty acids, used as energy reserves
  • Phospholipids have hydrophilic heads and hydrophobic tails, forming micelles in water
  • Proteins are made of amino acids linked by peptide bonds, with primary, secondary, tertiary, and quaternary structures
  • Primary structure is the order and number of amino acids, secondary structure includes alpha helix and beta pleated sheet formations
  • Tertiary structure is the 3D shape of the protein, globular proteins are compact and soluble, while fibrous proteins are long and insoluble
  • Quaternary structure consists of multiple subunits closely packed together, like in haemoglobin
  • Water is a polar molecule, a metabolite, solvent, and has high specific heat capacity and latent heat of vaporization
  • Water exhibits strong cohesion, supporting capillary action and high surface tension