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What is the except ot the rule that all amino acids are primary amino acids?
Proline
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Are all 20 AA's alpha amino acids?
Yes
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What configuration do all AAs have?
The L configuration
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What are amino acids joined together by?
Peptide bonds between alpha carboxyl and alpha amino groups join amino acids together
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What are the neutral amino acids?
Gly, Ala, Val, Leu, Ile
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What amino acids have hydroxyl groups?
Ser, Thr, (also Tyr - but not noted in lecture)
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What AA's contain sulfur?
Cys, Met
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What are the aromatic AA's?
Phe, Tyr, Trp
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What are the acidic AAs?
Aspn, Asn, Glu, Gln
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What are the basic AA's?
His, Arg, Lys
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What is the one imino acid?
Proline
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Does a strong acid have a high pKa or a low pKa?
A strong acid has a LOW pKa
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What is the zwitterionic form of an AA?
A + charged amino group and a - charged carboxyl. This is what is present at physiological pH.
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Do the side chains of Asn and Gln ionize?
No
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What AA has appreciable buffering capacity at physiological pH?
Histidine
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What is the MW of a protein that is 10 AA residues long?
10 x 110 = 1100 (use 110 for each AA)
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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)
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Addition of carbohydrates through serine and threonine is known as what?
O-linked glycosolation
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Addition of carbohydrates through asparagine is known as what?
N-linked glycosolation
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What determines the primary AA sequence?
- - nucleotide sequence
- - gene splicing
- - proteolytic processing
- - post-translational modification
- - covalent cross bridging
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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
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