1. Biological Molecules

Cards (83)

  • Monomer: smaller units that join together to form larger molecules
  • Examples of monomers:
    • Monosaccharides (glucose, fructose, galactose)
    • Amino acids
    • Nucleotides
  • Polymer: molecules formed when many monomers join together
  • Examples of polymers:
    • Polysaccharides
    • Proteins
    • DNA / RNA
  • Condensation reaction:
    • A chemical bond forms between 2 molecules
    • A molecule of water is produced
  • Hydrolysis reaction:
    • A water molecule is used to break a chemical bond between 2 molecules
  • Hexose monosaccharides:
    • Glucose
    • Fructose
    • Galactose
    • All have the molecular formula C6H12O6
  • Type of bond formed when monosaccharides react:
    • (1,4 or 1,6) glycosidic bond
    • 2 monomers = 1 chemical bond = disaccharide
    • Multiple monomers = many chemical bonds = polysaccharide
  • Disaccharides and how they form:
    • Maltose: glucose + glucose
    • Sucrose: glucose + fructose
    • Lactose: glucose + galactose
    • All have molecular formula C12H22O11
    • Formed through a condensation reaction that forms a glycosidic bond between 2 monosaccharides
  • Structure of α-glucose:
    • OH H
  • Structure and functions of starch:
    • Storage polymer of α-glucose in plant cells
    • Insoluble = no osmotic effect on cells
    • Large = does not diffuse out of cells
    • Amylopectin: 1,4 & 1,6 glycosidic bonds, branched
    • Amylose: 1,4 glycosidic bonds, helix with intermolecular H-bonds = compact
  • Structure and functions of glycogen:
    • Main storage polymer of α-glucose in animal cells (also found in plant cells)
    • 1,4 & 1,6 glycosidic bonds, branched
    • Insoluble = no osmotic effect & does not diffuse out of cells
    • Compact
  • Structure and functions of cellulose:
    • Polymer of β-glucose
    • Gives rigidity to plant cell walls
    • 1,4 glycosidic bonds
    • Straight-chain, unbranched molecule
    • Alternate glucose molecules are rotated 180°
    • H-bond crosslinks between parallel strands form microfibrils = high tensile strength
  • Benedict’s test for reducing sugars:
    1. Add an equal volume of Benedict’s reagent to a sample
    2. Heat the mixture in an electric water bath at 100 ℃ for 5 mins
    3. Positive result: colour change from blue to orange & brick-red precipitate forms
  • Benedict’s test for non-reducing sugars:
    1. Negative result: Benedict’s reagent remains blue
    2. Hydrolyse non-reducing sugars e.g. sucrose into their monomers by adding 1cm3 of HCl. Heat in a boiling water bath for 5 mins
    3. Neutralise the mixture using sodium carbonate solution
    4. Proceed with the Benedict’s test as usual
  • Test for starch:
    1. Add iodine solution
    2. Positive result: colour change from orange to blue-black
  • Colorimetry for qualitative results of sugars and starch:
    1. Make standard solutions with known concentrations. Record absorbance or % transmission values
    2. Plot calibration curve: absorbance or % transmission (y-axis), concentration (x-axis)
    3. Record absorbance or % transmission values of unknown samples. Use calibration curve to read off concentration
  • To test for lipids in a sample:
    • Dissolve solid samples in ethanol
    • Add an equal volume of water and shake
    • Positive result: milky white emulsion forms
  • Triglycerides form through a condensation reaction between 1 molecule of glycerol and 3 fatty acids forming ester bonds
  • Contrast between saturated and unsaturated fatty acids:
    Unsaturated:
    • Contain C=C double bonds
    • 'Kinked' molecules have fewer contact points
    • Lower melting point = liquid at room temperature
    • Found in plant oils
    Saturated:
    • Contain only single bonds
    • Straight-chain molecules have many contact points
    • Higher melting point = solid at room temperature
    • Found in animal fats
  • Structure of triglycerides related to functions:
    • High energy:mass ratio = high calorific value from oxidation (energy storage)
    • Insoluble hydrocarbon chain = no effect on water potential of cells & used for waterproofing
    • Slow conductor of heat = thermal insulation e.g. adipose tissue
    • Less dense than water = buoyancy of aquatic animals
  • Structure and function of phospholipids:
    • Amphipathic molecule: glycerol backbone attached to 2 hydrophobic fatty acid tails & 1 hydrophilic polar phosphate head
    • Forms phospholipid bilayer in water = component of membranes
    • Tails can splay outwards = waterproofing
  • Comparison between phospholipids and triglycerides:
    • Both have glycerol backbone
    • Both may be attached to a mixture of saturated, monounsaturated & polyunsaturated fatty acids
    • Both contain the elements C, H, O
    • Both formed by condensation reactions
  • Contrast between phospholipids and triglycerides:
    Phospholipids:
    • 2 fatty acids & 1 phosphate group attached
    • Hydrophilic head & hydrophobic tail
    • Used primarily in membrane formation
    Triglycerides:
    • 3 fatty acids attached
    • Entire molecule is hydrophobic
    • Used primarily as a storage molecule (oxidation releases energy)
  • Water and inorganic ions are not polymers; they are macromolecules
  • Water is a polar molecule because O is more electronegative than H, forming O 𝛿 - (slight negative charge) & H 𝛿 + (slight positive charge)
  • Biologically important properties of water:
    • Metabolite/solvent for chemical reactions in the body
    • High specific heat capacity
    • High latent heat of vaporization
    • Cohesion between molecules
  • Water is significant to living organisms because it is a solvent for polar molecules during metabolic reactions, enables organisms to avoid fluctuations in core temperature, and provides cohesion-tension of water molecules in the transpiration stream
  • Inorganic ions do not contain carbon atoms and are found in cytoplasm & extracellular fluid in high or very low concentrations
  • Role of hydrogen ions in the body:
    • High concentration of H+ = low (acidic) pH
    • H+ ions interact with H-bonds & ionic bonds in tertiary structure of proteins, which can cause them to denature
  • Role of iron ions in the body:
    • Fe2+ bonds to porphyrin ring to form haem group in haemoglobin
    • Haem group has binding site to transport 1 molecule of O2 around body in bloodstream
    • 4 haem groups per haemoglobin molecule
  • Role of sodium ions in the body:
    • Involved in co-transport for absorption of glucose & amino acids in lumen of gut
    • Involved in propagation of action potentials in neurons
  • Role of phosphate ions in the body:
    • Component of DNA, ATP, NADP, cAMP
  • General structure of an amino acid:
    • COOH: carboxyl/carboxylic acid group
    • R: variable side group consists of carbon chain & may include other functional groups e.g. benzene ring or -OH (alcohol)
    • NH2: amine/amino group
  • Test for proteins in a sample:
    • Biuret test confirms presence of peptide bond
    • Add equal volume of sodium hydroxide to sample at room temperature
    • Add drops of dilute copper (II) sulfate solution. Swirl to mix
    • Positive result: colour changes from blue to purple
    • Negative result: solution remains blue
  • Number of amino acids: 20 differ only by side 'R' group
  • Formation of dipeptides and polypeptides:
    • Condensation reaction forms peptide bond (-CONH-) & eliminates molecule of water
    • Dipeptide: 2 amino acids
    • Polypeptide: 3 or more amino acids
  • Levels of protein structure: 4
  • Primary structure of a protein:
    • Sequence, number & type of amino acids in the polypeptide
    • Determined by sequence of codons on mRNA
  • Secondary structure of a protein:
    • Hydrogen bonds form between O 𝛿- (slightly negative) attached to ‒ C=O & H 𝛿+ (slightly positive) attached to ‒NH