Chpt 2

Cards (62)

  • protists = large groups of mostly single-celled organisms that cannot be classified as a plant, animal or fungus that have similar characteristics
  • organic molecules are complex that are derived from or produced by living organisms and have carbon-hydrogen bonds
  • inorganic molecules are simple and are derived from non-living components and have no carbon-hydrogen bonds
  • carbohydrates role:
    • important source of chemical energy
    • energy reserves in plants and animals
    • form structural components
    • form part of RNA and DNA
  • three main groups of carbohydrates - monosaccharides, disaccharides, polysaccharides
  • lipids role:
    • main component of the plasma and organelle membrane
    • storing energy
    • hormones
  • lipids are insoluble to water
  • two general forms of lipids - simple and compound
  • protein functions:
    • catalyse cellular reactions
    • hormones
    • act as carrier molecules
    • form structural components in organisms (collagen)
  • a protein is formed by one or more polypeptide chains in a biologically functioning way
  • protein = fully functioning molecule
  • polypeptide = non-functioning
  • nucleus = double membrane, contains genetic information, directs cell activity
  • mitochondrion = double membrane, release energy from organic compounds (cellular respiration)
  • rough endoplasmic reticulum = membrane bound, synthesises and processes proteins
  • ribosome = non-membrane bound, composed of proteins and ribosomal RNA, synthesises proteins
  • Golgi apparatus = membrane bound, further processes and packages proteins into vesicles for export from the cell
  • chloroplast = double membrane, photosynthesis
  • proteome = all the proteins present in a cell or organism
  • the structure of proteins - atomic level - proteins are made up of carbon, hydrogen, oxygen, nitrogen and sometimes sulphur
  • proteins are made of smaller amino acids, when they joined together they lose a water molecule in a reaction called condensation reaction
  • examples of proteins:
    • keratin is a structural protein -> hair, nails, skin
    • haemoglobin is a transport protein that carries oxygen from lungs to the rest of the body
    • lactase -> enzyme that breaks down lactose
  • all amino acids have:
    • an amine group (NH2)
    • carboxyl group (COOH)
    • variable R group (or side chain)
  • 2 of the 20 different amino acids contain sulfur
  • the R group gives the amino acid a name
  • amino acids have different properties, basic, polar, non-polar, acidic
  • proteomics = large scale study of the structure, function, and interactions of proteins
  • enzymes act as a biological catalyst in metabolic reactions
  • anabolic reactions = reactions that make larger molecules
  • catabolic reactions = reactions that break down larger molecules into smaller molecules
  • polypeptide chain = chain of amino acids joined by peptide bonds
  • during condensation, monomers (amino acids) are linked via strong covalent bonds and a water molecule is released
  • covalent bond can be broken by a hydrolosis reaction
  • hydrolosis reaction = addition of a water molecule
  • Primary structure of a protein
    • sequence of amino acids that make 2D polypeptide chain
    • genes determine order and number of amino acids
    • linear sequences shorter than 50 amino acids are peptides
    • the linear sequence provides information on how proteins will fold
  • secondary structure of a protein
    • predictable repeating pattern of alpha helices and beta pleated sheets due to hydrogen bonding between peptide bonds
    • random coiling is another secondary structure
  • tertiary structure of a protein
    • 3D structure where the polypeptide chain folds in due to the various chemical reactions between R groups
    • different areas are affected by the R groups
    • folding process occurs spontaneously in some smaller polypeptides
    • larger proteins need specialised proteins to fold correctly
  • quaternary structure of a protein
    • level of structure in which two or more polypeptide chains or prosthetic groups bond together to form a 3D structure
    • only some proteins have a quaternary structure (haemoglobin)
    • chaperonins help with folding
  • prosthetic groups = an inorganic compound that is involved in protein structure or function
  • conjugated protein = a protein with a prosthetic group eg haemoglobin