Respuesta :
Answer:
The amino sequence of an octapeptide can be determined by :
i.Amino acids present in the peptide
ii.By the behaviour shown by the treatment of these material with different biological and chemical reactions
As shown ammonium was released from the peptide,which shows that the peptide contains either Asn or Gln.
As there is presence of Asp in the amino acid analysis which indicates that the octapeptide contains Asp.
Acid hydrolysis hydrolyzes the peptide bonds which yields a Ala-Val which is the result of partial acid hydrolysis.
Chymotrypsin is on the C-terminal side of the aromatic amino acids Phe, Tyr, and Trp. The peptide has Tyr which indicates that the two present tetrapeptides after chymotrypsin treatment are fourth and eighth amino acids i-e N--Tyr-C and Tyr as the fourth amino acid and Ala-Val somewhere in the octapeptide
As Arg is only present on the C terminal side of the Trypsin cleavage therefore Arg must be the second or the sixth amino acid for the two dipeptides to form as a result of arginine treatment of a tetrapeptide
Cyanogen bromide cleaves on the C-terminal side of Met residues. For free Tyr to be produced from cyanogen bromide treatment of one of the tetrapeptides, Met must be either the third or seventh amino acid. Because Ala was present in both tetrapeptides, Ala must be either the first or fifth amino acid, present in the same tetrapeptide as Arg and Met,i-e N.-Tyr-C and Ala-Val somewhere in the octapeptide and Ala-Arg-Met as the first, second, and third or fifth, sixth, and seventh amino acids and Tyr as the fourth amino acid.
One of the tetrapeptides contains Ala-Val as its second and third amino acids and Asn as its N-terminal amino acid. Therefore two combinations are possible as below
N-Asn-Ala-Val-Tyr-Ala-Arg-Met-Tyr-C or N-Ala-Arg-Met-Tyr-Asn-Ala-Val-Tyr-C
Answer:
The amino aciid sequence of an octapeptide can be determined from the amino acids that are present in the peptide and from the results of different chemical and biological treatments.
One equivalent of ammonium was released fro the peptide, indicating that the peptide contains either Asn or Gln. The presence os Asp in the amino analysis indicates that the octapeptide contains Asn.
A) Acid hydrolysis hydrolyzes peptide bonds. The dipeptide Ala-Val is obtained by partial acid hydrolysis. The indicates that Ala-Val is present in the peptide
B) Chymotrypsin cleaves on the C-terminal side of the aromatic amino acids. Phe, Tyr, and Trp. The peptide contains only Tyr. The presence of tetrapeptides after the treatment of ohymotrypsin indicates that Tyr is the fourth and eighth amino acids.
N-Tyr-C and Tyr present as the fourth amino acid. in constrast, Ala-Val is present in the octapeptide
C) Trpsin cleaves on the C-terminal side of Arg and Lys residues. only Arg is present in the octapeptide. Arg must be the second or sixth amino acid, for two dipeptide to be formed from arginine during the treatment of one tetrapeptide.
D) Cyanogen bromide cleaves on the C-terminal side of Met residues. For free Tyr to be produced from cynogen bromide treatment of one of the tetrapeptides, Met must be either the third or seventh amino acid. Because Ala is present in both tetrapeptides, Ala must be either the first or fifth amino acid, present in the same tetrapeptide as Arg and Met.
In addition, presence of N-...-Tyr-C and Ala-Val in the octapeptide and Ala-Arg-Met as the first, second, third or fifth, sixth or seventh amino acids and Tyr as the fourth amino acid.
E) One of the tetrapides contains Asn as its N-terminal amino acid, and Ala-Val as its second and third amino acids. Two octapeptides are possible from this peptide analysis.
The amino acid sequence of the octapeptide is the following:
N-Asn-Ala-Val-Tyr-Ala-Arg-Met-Tyr-C:
N-Ala-Arg-Met-Tyr-Asn-Ala-Val-Tyr-C:
For more information visit,
https://brainly.com/question/18122741
