MBOD - Primary Structure of Proteins
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What is the except ot the rule that all amino acids are primary amino acids?
Are all 20 AA's alpha amino acids?
What configuration do all AAs have?
The L configuration
What are amino acids joined together by?
Peptide bonds between alpha carboxyl and alpha amino groups join amino acids together
What are the neutral amino acids?
Gly, Ala, Val, Leu, Ile
What amino acids have hydroxyl groups?
Ser, Thr, (also Tyr - but not noted in lecture)
What AA's contain sulfur?
What are the aromatic AA's?
Phe, Tyr, Trp
What are the acidic AAs?
Aspn, Asn, Glu, Gln
What are the basic AA's?
His, Arg, Lys
What is the one imino acid?
Does a strong acid have a high pKa or a low pKa?
A strong acid has a LOW pKa
What is the zwitterionic form of an AA?
A + charged amino group and a - charged carboxyl. This is what is present at physiological pH.
Do the side chains of Asn and Gln ionize?
What AA has appreciable buffering capacity at physiological pH?
What is the MW of a protein that is 10 AA residues long?
10 x 110 = 1100 (use 110 for each AA)
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)
Addition of carbohydrates through serine and threonine is known as what?
Addition of carbohydrates through asparagine is known as what?
What determines the primary AA sequence?
- - nucleotide sequence
- - gene splicing
- - proteolytic processing
- - post-translational modification
- - covalent cross bridging
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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