Biochemistry Test 1

  1. Which forces stabilize the quaternary structures of proteins?
    Hydrophobic effect, Ionic Bonding, Hydrogen Bonding, van der Walls forces, and Disulfide Bonding.
  2. Where does F1-ATPase exist?
  3. What is the function of F1-ATPase?
    Responsible for generationg ATP from ADP in mitochondria.
  4. What is an amphipathic alpha-helix?
    Contains hydroPHOBIC residues on one side of the chain and hydroPHILIC residues on the other side.
  5. When 2 or more amphipathic alpha-helices associate along their long axis, they form...
    A coiled coil.
  6. The interior of BILOGICAL membranes are composed of __________ fatty acid chains.
  7. What are the 3 dynamic properties of proteins?
    Atomic Fluctuations, Collective Motions (breathing), and Triggered Conformational Changes.
  8. What are the transmembrain proteins that form conducting pores through the lipid bilayer of cells?
    Ion Channels
  9. What is an environmentally-induced fluctuation in the struction and function of ion channel proteions called?
  10. What is a stimulated, long-range structural alteration that leads to functional changes in a proteins properties called?
  11. Channels undergo allosteric changes to convert between conducting and nonconducting states. What is this?
  12. What is it when ion channels open to conduct ions?
  13. What is it when ion channels close to block conduction?
  14. What is it when ion conduction is blocked rapidly following channel activation?
  15. What is an apo-conformation?
    An unbound state.
  16. ____________ only happens when Neurotransmitter-gated ion channels open and close after a receptor is excited for a "long" period of time.
  17. What is the Michaelis-Menten equation?
    V/Vmax = s/s+Km
  18. A protein that has little or no enzymatic activity; but once it is processed posttranslationally, it become competent for catalysis.
    Zymogen or Proenzyme
  19. The small group of catalytic RNAs that can catalyze chemical reactions.
  20. An organic, non-peptidicmolecule that needs to bind an enzyme so that the enzyme can catalyze a chemical reaction.
    Coenzymes or Cofactors
  21. The term ________________ imples that the coenzyme is tightly or covalently bound to the enzyme and does not dissociate from the enzyme during catalysis.
    prosthetic groups
  22. A coenzyme-dependent enzyme that does not have a coenzyme bound to it and needs something to work properly.
  23. An enzyme that has its coenzyme tightly bound to it.
  24. Enzymes that catalyze the same reaction yet differ in their amino acid sequence.
    Isozyme (isoenzyme)
  25. A _____________ starts with the binding of substrate and ends with the release of product and formation of the enzyme in its initial state, for instance.
    catalytic cycle
  26. One ___________ is usually the amount of enzyme that produced 1 umol of product per minute.
    enzyme unit (U)
  27. As Km goes up, [substrate] _______.
    goes up, as well
Card Set
Biochemistry Test 1
The first few terms that I should know for Biochem.