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BIOCHEM ONE - Review

  1. How do enzymes affect reactions?
    • Faster Rate
    • Milder Conditions
    • Greater Specificity
    • Regulatable
  2. What two features of Subtrate Binding Sites (Enzymes) need to be complimentary?
    • Shape
    • Charge (Surface Potentials)
  3. Define,
    Holoenzyme.
    Apoenzyme.
    • Holoenzyme - Enzyme + Cofactor (Active)
    • Apoenzyme - Enzyme without cofactor (Inactive)
  4. How are enzymatic reactions controlled?
    • Vary amt. of enzyme
    • Directly control enzyme (with effector)
  5. What types of enzyme modifications affect activity?
    • Covalent Binding
    • Non-covalent Binding
  6. Define Allostery.
    • Binding at an Effector Site alters binding of a Different ligand at the Functional (Active) Site.
  7. Define Cooperativity.
    Binding of a Ligand at a Functional Site alters binding of the same ligand at other Functional Sites
  8. Define the Terms,
    Heterotropic
    Homotropic
    • Heterotropic - Effectors are different from ligand/subtrate
    • Homotropic - Effectors are same as ligand/substrate
  9. Define the terms (with regards to enzyme effectors),
    Activator
    Inhibitor
    • Increases Substrate binding affinity
    • Decreases Substrate binding affinity
  10. What is a Domain?
    A structurally independant unit with characteristics of small globular proteins
  11. What is an α+β domain?
    An Antiparallel beta sheet
  12. What is a salt bridge? What are the other two similar types of interaction?
    • A salt bridge is an electrostatic polypeptide attraction between polar charged residues.
    • Ion-Dipole, Dipole-Dipole and Van Der Waals are the other types of interaction
  13. What are Hyrdogen Bonding and Hydrophobic effect ineractions?
    • Hydrogen Bonding is between species with acidic and basic character
    • Hyrdophobic effect is the interaction of Nonpolar residues with water
  14. What factors can denature proteins?
    • pH
    • Detergent
    • Chaotropic Salts
    • Temperature
    • Certain Water Soluable Organics
  15. Protein Primary Structure
    Sequence of residues
  16. Protein Secondary Structure
    Local Spatial Conformation of Backbone
  17. Protein Tertiary Structure
    Overall 3D arrangement of polypeptide
  18. Quaternary protein structure
    Spatial arrangement of subunits in a multisubint protein
  19. Neutral Drift
    Random mutations in well adapted proteins that do not affect function
  20. Homologous
    Evolved or derived from a common ancestor
Author
Ant
ID
241200
Card Set
BIOCHEM ONE - Review
Description
Biochem
Updated

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