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Drawing Structures of Tetrapeptides

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How to draw the structure of this tetrapeptide:


What type of bonding between amino acid residues is most important in holding a protein and polypeptide in a specific secondary configuration?

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Since alanine is listed first, this one must be the N-terminal. That means that it will expose its free NH2 group. Since threonine is listed last, it is the C-terminal. That means that it will have its COOH group free and exposed. We know this because primary structure of proteins are always listed with the N-term first.

The other piece of information we need is ...

Solution Summary

This solution explains structures of tetrapeptide and describes bonding between amino acids.

See Also This Related BrainMass Solution

Determining amino acid sequences of peptide and octapeptide

1. What is the amino acid sequence of the peptide?

The complete hydrolysis of an unknown nonapeptide revealed the presence of Glu, Val, Val,Gly,Lys, Lys, Tyr, Thr and Phe residues.
The first amino acid to be detected as a phenylthiohydantoin derivative on Edman degradation of the peptide was glutamic acid.
The only amino acid detected after treating the peptide with hydrazine (converts all amino acids except the C-terminus into acyl hydrazines)was threonine.
Treatment of the peptide with trypsin (cleaves on the carboxyl side of lys and arg) and chymotrypsin (cleaves carboxyl side of aromatic amino acid)gave three fragments in each case. T1, T2, T3 and C1, C2, C3 respectively. None of the trypsin fragments was identical to the chymotrypsin fragments.
C2 and T2 proved to be dipeptides;C1 and T1 were tripeptides and C3 and T3 were tetrapeptides
The N-terminal residue of T3 was shown to be phenylalanine and the C-terminus threonine.
The N-terminus of C1 was glycine and C-Terminus was the same as in T3.
C2 was shown to contain tyrosine and glutamic acid.
T1 was composed of lysine, tyrosine, and glutamic acid.
The N-terminus of T2 was valine
The N-terminus of C3 was lysine
At basic Ph the C3 fragment migrated with a net charge of +2

2. Determine the amino acid sequence of an octapeptide that was found to contain GLY, GLy, ASP,CYS,LYS,MET,ASN, and ARG. from the information given below
A. The intact peptide was treated with cyanogen bromide (cleaves on carboxyl side of methionine) and two fragments were detected. One of the fragments was reacted with phenylisothiocyanate followed by an acid work-up. The cyclic phenythiohydantoin amino acid that was released from the residue was found to contain Asparagine.
B. Another sample of the octapeptide was reacted with hydroxylamine (cleaves Asparagine-Glycine bonds) and again two fragments were detected. One of the fragments was determined to be three residues long by gel filtration chromatography.
C. The octapeptide was then treated with Trypsin (cleaves on carboxyl side of arginin andn lysine) which resulted in three fragments. One of the fragments was determined by paper chromatography to be Lysine. One of the other fragments was determined to be two residues long and when subjected to electrophoresis in the horizontal direction placed in an atmosphere of per formic acid, and eletrophoresed in the vertical direction, it was found to lie off the diagonal.
D. Finally, 2-nitro-5-thiocyanobenzoate (amino side of cysteine) was reacted with the original peptide and two fragments resulted. One of the fragments contained two residues, which gave the same results as in #3 when subjected to diagonal electrophoresis. This same two-residue fragment also sticks on a column that has diethylaminoethyl (DEAE) groups attached to an immobile resin, when the Ph is 7

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