Chem3BProteins

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Author:
victimsofadown
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85153
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Chem3BProteins
Updated:
2011-05-16 13:26:39
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Chem3BProteins
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Chem3BProteins
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  1. Protein structure (linkage)? Functions?
    • condensation polymers, polyamide of amino acids (aka peptide bonds)
    • Structure, contraction (myofilament), transport (hemoglobin), energy storage, hormones (GH, insulin), enzymes, protections (IgE)
  2. General amino acid structure. α, ϐ, etc? L vs R?
    • α, ϐ, etc refer to C that amine is located on. Proteins use α amino acids
    • L/R refer to location of NH2 group
    • L amino acids are "natural"
  3. # of amino acids? Essential?
    • 20
    • 10
  4. Categories of amino acids w/ types of R groups and pI
    • Nonpolar (neutral): hydrocarbon, benzene ring; pI 6
    • Polar (neutral): SH, OH, amide; pI 6
    • Acidic: additional COOH; pI 3
    • Basic: additional NH2; pI 10
  5. pI
    isoelectric point - The pH at which the zwitterion is formed
  6. zwitterion form
    • Net charge = 0
  7. Neutral, acidic, and basic amino acids at pH 1, 3, 6, 10, 12
    • Neutral: 1 (+1), 3 (+1), 6 (0), 10 (-1), 12 (-1)
    • Acidic: 1 (+1), 3 (0), 6 (-1), 10 (-2), 12 (-2)
    • Basic: 1 (+2), 3 (+2), 6 (+1), 10 (0), 12 (-1)
  8. How would each type of amino acid react in electrophoresis, gel pH 6?
    • Neutral AA (no charge) - stays stationary
    • Acidic AA (negative) - moves toward cathode
    • Basic AA (posative) - moves toward anode
  9. Terminals
    • N-terminus: NH2 end of amino acid
    • C-terminus: COOH end of amino acid
  10. Various lengths of amino acids and names
    • 1-8 C: dipeptide, tripeptide,..., octapeptide
    • 9-19 C: oligopeptide
    • 20-49 C: polypeptide
    • 50+ C: protein
  11. How are amino acid sequences written? How to determine amount of possibilities?
    • sequenced in order, left to right (N-terminus on left)
    • Total amount of possabilities = n! where n = # of amino acids
    • n! = n·(n-1)·(n-2)·(n-3)·,...,·1)
  12. Primary protein structure
    • Number, type, and sequence of AA
    • Determined by applying HCl to protein which breaks all bonds allowing determination of number and type of AA.
    • Other chemicals react with different AAs to produce varied lengths and breakages, a combination of this information will lead to the correct sequence
  13. Secondary Protein Structure
    • H bonding in the back bone
    • Alpha helix - every 3-5C H-bonding between carbonyl and amine of another AA
    • Beta pleated sheet - A sort of "bent" alpha helix
  14. Tertiary structure
    • vanderwalls, H bonding, disulfide bridge, electrostatic interactions (between R groups)
    • Gives overall 3D form with hydrophobic R facing in and hydrophilic R facing out
  15. Quaternary Structure
    Van der walls, H bonding, electrostatic interactions (between multiple tertiary structures)

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