Please explain your steps Thank You 4 The sequence of a pept

Please explain your steps. Thank You!

4.) The sequence of a peptide is discerned through proteoolytic analysis. Cleavage with trypsin gives: LCR, FACK, YHCK, IVIR, VWPR and cleavage with chymotrypsin gives Y, CR, PRL, ACKVW, HCKIVIRF.

a.) What is the sequence of the intact peptide?

b.) this peptide is held together by one disulfide bond Clipping the peptide with trypsin, followed by hydrolosis and amino acid analysis gives back all the amino acids in the peptide. Show the placement ofthe disulfide bond.

5.) Conside this peptide: ESTGGEYHAIFKMPYKR

a.) Show the full 3D structure at physiological pH for the 3- amino acid fragement that results from clipping the peptide with thermolysin.

b.) Estimate the pI of this peptide within 0.2 units

Can you also please answer questions from the following link. Thanks a lot!!

https://drive.google.com/file/d/0B_J-3r9hINYlcldIYmcwN3haX3dRYWxIQVVISS1XdjZfZGRn/view?userstoinvite=ihussein@terpmail.umd.edu&ts=58b34d87&actionButton=1

The sequence of a peptide is discerned through proteolytic digest analysis Cleavage with trypsin gives LCR, FACK, YHCK, IVIR, VWPR, and Cleavage with chymotrypsin gives Y, CR, PRL, ACKVW HCKIVIRF Place the sequence of the intact peptide in the box provided. This peptide is held together by one disulfide bond Clipping the peptide with trypsin, followed by hydrolysis and amino acid analysis gives back all the amino acids in the peptide! Show the placement of the disulfide bond in the box provided! consider this peptide: ESTGGEYHAIFKMPYR. Show the full 3D structure at physiological pH for the 3amino acid fragment that results from clipping the peptide with thermolysin. Estimate the pI of this peptide within 0.2 units _________ Indicates it\'s charge at pH 9.0 +/-0.1 units ________

Solution

(a). The sequence of intact peptide is YHCKIVIRFACKVWPRLCR

(b) Disulfide bond is formed between cysteine amino acid lies just after histidine and the cysteine amino acid lies just after alanine of the peptide chain.

5. Since thermolysine preferably clevage the peptide chain on the location where aromatic amino acids found.

Aromatic amino acids like Isoleucine, lysine, Valine, Methionine, Alanine and Phenylalanine. So, in the given peptide chain, thermolysine with cleavage the peptide with IFK.