Bio lecture 2/3 quiz 1

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  1. Polymer
    • •made of amino acid subunits (monomers)
    • Book def is Any long molecule composed of  small repeating units bonded together.
  2. Amino acid
    A small organic molecule with a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom and a side group. Proteins are polymers of 20 common amino acids. (side chain is what differs between types of amino acid)Image Upload 1
  3. Peptide bond
    covalent bond between carboxyl group of one amino acid and the amino group of the amino acid next to it. (Covalent Bond) Image Upload 2
  4. 4 basic levels of organization of protein structures.
    • Primary
    • Secondary
    • Tertiary
    • Quaternary
  5. Primary Structure
    sequence of amino acids (order matters)!!
  6. What if primary structure changes?
    Each amino side chain has specific properties. The change of a single amino acid would change the function. Example is sickle cell disease.
  7. Secondary Structure
    • results from hydrogen bonding between the carboxyl oxygen of one amino acid and the amino hydrogen of another. This is where the structure starts to becomes more 3-d like. Image Upload 3
    • Alpha helix is spirally Beta sheets are more straight.
  8. Alpha Helix / Beta sheets
    • Proteins can have these multiple secondary structures.
    • Image Upload 4
  9. Tertiary Structure
    interactions involving amino acid side chains. Hydrogen bonds / hydrophobic interactions. Hydrophobic parts will start to fold inside cause fuck that water.
  10. Image Upload 5Quaternary structure
    2 or more protein subunits will form a single functional protein.
  11. Structure summary
    Image Upload 6 Primary, secondary, tertiary, Quaternary (happens all at once.)
  12. Molecular chaperones
    Proteins that help other proteins fold
  13. Denatured
    Not functioning
  14. Will proteins function if they are not folded?
    No. Proper folding is required for functioning
  15. Enzymes
    • Most proteins function as enzymes.
    • They start chemical reactions, lower activation energy and are not consumed in the reaction.
    • Image Upload 7 without enzyme
    • Image Upload 8 with enzyme
  16. Temperature affects on enzyme function
    • movement of substrates and enzyme
    • enzyme shape
    • Certain types of enzymes do better in specific temperatures.
  17. pH affects on enzyme function
    • enzyme shape
    • ideal temp and pH depends on environment of organism.
  18. Substrate
    They are reactants that bind to active site of enzyme. enzyme binds only specific substrates.. not just to anything. Image Upload 9
  19. Steps of enzymatic catalysis
    • 1. reactants bind to the active site
    • 2.interactions between the substrate and active site lower the activation energy.
    • 3. Reaction products are released from the enzyme.
  20. Coenzymes / cofactors
    additional factors required for normal enzyme function. (such as vitamins and minerals.)
  21. Competitive inhibition
    • molecules similar in size and shape to the substrate will compete with the substrate for active site binding. This is a way to turn unneeded enzymes off "binds and blocks"
    • Image Upload 10
  22. Allosteric Regulation
    • Molecule causes a change in enzyme shape by binding to the enzyme at a location other than the active site. closes enzyme active site, but can be reopened by other regulatory molecules.
    • Image Upload 11
  23. Biochemical Pathway
    • Series of enzymatic reactions
    • Product of reaction one becomes substrate of reaction two...
  24. Feedback inhibition
    • a regulation method for biochemical pathways.
    • If final product is abundant they don't waste energy by making more.  Final product will bind to first enzyme to shut down chain. Can be restarted if more product is needed.
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Bio lecture 2/3 quiz 1
2013-01-24 15:11:09
quiz proteins enzymes

Lecture 2 enzyme action bio 102
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