MBOD - Primary Structure of Proteins

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MBOD - Primary Structure of Proteins
2010-09-02 08:47:36
primary protein structure

MBOD - Primary Structure of Proteins
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  1. What is the except ot the rule that all amino acids are primary amino acids?
  2. Are all 20 AA's alpha amino acids?
  3. What configuration do all AAs have?
    The L configuration
  4. What are amino acids joined together by?
    Peptide bonds between alpha carboxyl and alpha amino groups join amino acids together
  5. What are the neutral amino acids?
    Gly, Ala, Val, Leu, Ile
  6. What amino acids have hydroxyl groups?
    Ser, Thr, (also Tyr - but not noted in lecture)
  7. What AA's contain sulfur?
    Cys, Met
  8. What are the aromatic AA's?
    Phe, Tyr, Trp
  9. What are the acidic AAs?
    Aspn, Asn, Glu, Gln
  10. What are the basic AA's?
    His, Arg, Lys
  11. What is the one imino acid?
  12. Does a strong acid have a high pKa or a low pKa?
    A strong acid has a LOW pKa
  13. What is the zwitterionic form of an AA?
    A + charged amino group and a - charged carboxyl. This is what is present at physiological pH.
  14. Do the side chains of Asn and Gln ionize?
  15. What AA has appreciable buffering capacity at physiological pH?
  16. What is the MW of a protein that is 10 AA residues long?
    10 x 110 = 1100 (use 110 for each AA)
  17. What are some examples of covalently modified AAs?
    • - Hydroxylation of proline in collagen
    • - Gamma carboxylation of glu (prothrombin)
    • - phosphorylation of serine / threonine (takes place on hydroxyl groups)
  18. Addition of carbohydrates through serine and threonine is known as what?
    O-linked glycosolation
  19. Addition of carbohydrates through asparagine is known as what?
    N-linked glycosolation
  20. What determines the primary AA sequence?
    • - nucleotide sequence
    • - gene splicing
    • - proteolytic processing
    • - post-translational modification
    • - covalent cross bridging
  21. What does primary AA sequence give rise to?
    • Folding pattern of polypeptide chain ->
    • configuration of chemical groups on polypeptide surface ->
    • binding of other peptides ->
    • physiological function of protein