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6. Saturated means?

  • No double bonds between Carbons
  • Not the max number of Hydrogen
  • Presence of double bonds

7. Aldehyde/Ketone group reacts with ? closing the ring.

  • Hydroxyl group
  • Carboxyl group
  • Carbonyl group

8. What is the effect on Km of a Non-competitve inhibitor?

  • Decrease
  • No Change
  • Increase

9. Which has the fatty acid with two Hydrogen atoms on the same side?

  • Cis
  • Trans

10. Breaking down, dipeptide into two amino acids.

  • Catabolism
  • Anabolism

11. Which one of these is not a way by which enzymes catalyse reactions?

  • Enzyme side chains act as acids/bases
  • Covalent bond in transition state
  • Donate fucntional groups for the product
  • Bring reactants into proximity

12. What change in energy makes for a spontaneous reaction?

  • Net negaitve change in free energy
  • Net positve change in free energy

13. Amino acids are Amphoteric.. what is this?

  • Have both basic and acidic groups
  • They are in a ring structure
  • They readily react

14. How many amino acids are coded for in our bodies?

  • 20
  • 200
  • 2

15. The sequnece of amino acids

  • Quternary
  • Primary
  • Tiertiary
  • Secondary

16. What is a heteropolymer?

  • A polymer with the same monomers
  • A polymer with 2 or more different monomers
  • A polymer with all glucose monomers

17. What bonds form between water molecules?

  • Electrostatic
  • Hydrogen Bonds
  • Van Der Waals

18. 3D structure determined by bonds and chaperone proteins?

  • Quaternary
  • Primary
  • Tiertiary
  • Secondary

19. Dimers, Trimers, tetramers?

  • Quaternary
  • Tiertiary
  • Primary
  • Secondary

20. Why are Electrostatic interactions important?

  • Stop the wrong cells from binding
  • For Protein surface, bind together (enzymes)
  • Keep us standing up