The peptide bond is a acid sensitive species. When it is subjected to the acid hydrolysis, the peptide bond(Amide bond) get hydrolysed into their respective amino and carboxylic group giving the... products as individuals Amino Acids.
Hence, the correct option is (C).
If the peptide Cys-Gly-Phe-Lys-Ala-Arg-Asp-Gly is subjected to acid hydrolysis, what will be the products? peptide fragments...
What fragments will be obtained by a trypsin hydrolysis of the following octapeptide? Ala-Val-Trp-Lys-Phe-Gly-Arg-Met A) Ala-Val-Trp-Lys-Phe and Gly-Arg-Met 3) Ala-Val-Trp-Lys-Phe-Gly and Arg-Met - Ala-Val-Trp-Lys and Phe-Gly-Arg and Met ) Ala-Val-Trp-Lys and Phe and Gly-Arg and Met ) Ala-Val-Trp and Lys-Phe-Gly and Arg-Met Bradykinin is a nonapeptide, Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg. In addition to one mole of Arg, what peptides are present after hydrolysis of bradykinin with chymotrypsin? A) Arg-Pro-Pro and Gly-Phe and Ser-Pro-Phe B) Pro-Pro-Gly and Phe-Ser-Pro-Phe-Arg C) Arg-Pro-Pro-Gly-Phe and Ser-Pro-Phe ?) Arg-Pro-Pro-Gly-Phe-Ser...
please explain each question thoroughly. thanks Question 3: Arg-Cys-Met-Ala-Cys-Gly-Arg-Pro-Asn-Tyr-Leu-Trp-Ala-Ile-His-Phe-Ser-Cys-Lys a. What would happen if this peptide were to be incubated with dinitrofluorobenzene (FDNB) followed by 6M HCl hydrolysis at 1100C for 24 hrs. What labeled product(s) would be detected? Consider the following pepide: What would happen if the peptide were treated with CNBr? What would the products be? Why? b. What would happen if the peptide were treated with chymotrypsin? What would the c. products be? Why? Arg-Cys-Met-Ala-Cys-Gly-Arg-Pro-Asn-Tyr, Leu-Trp, Ala-Ile-His-Phe,...
What peptides are expected to be produced when an unknown hormone (Cys−Ala−Phe−Met−Gly−Asp−His−Arg−Ala−Cys−Lys−Pro−Val) is cleaved by: a) trypsin b) cyanogen bromide c) thermolysin
5. Consider the following peptide: His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gin- Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr a. What are the fragments, if it is cleaved by trypsin? b. What are the fragments, if it is cleaved by chymotrypsin? c. What are the fragments, if it is cleaved by pepsin?
Which of these protein sequences is most likely to span a cell membrane? Gly-Asp-Val-Ala-Gly-Arg-Gly-Asn-Gly-Lys-Lys-Pro-Ser-Ser-Val-Arg-Ala-Leu-Ser Ile-Val-Leu-Pro-Ile-Val-Leu-Leu-Val-Phe-Leu-Cys-Leu-Gly-Val-Phe-Leu-Leu-Trp Lys-Asn-Trp-Arg-Leu-Lys-Asn-Ile-Asn-ser-Ile-Asn-Phe-Asp-Asn-Pro-Val-Tyr-Gln A. 773 B. 792 C. 811
Complete hydrolysis of an unknown basic decapeptide gives Gly, Ala, Leu, Ile, Phe, Tyr, Glu, Arg, Lys, and Ser. Problem 24-44 ConstantsI Periodic Table Complete hydrolysis of an unknown basic decapeptide gives Gly, Ala, Leu, lle, Phe, Tyr, Glu, Arg, Lys, and Ser. Terminal residue analysis shows that the N terminus is Ala and the C terminus is lle. Incubation of the decapeptide with chymotrypsin gives two tripeptides, A and B, and a tetrapeptide, C. Amino acid analysis shows that...
please help!!! 19. A peptide is composed of the following amino acids: Ala, Arg. Glu, Gly, Lys, Met, Phe, Ser, Tyn Given the following data deduce the sequence of the peptide. Trypsin digestion yielded two fragments with the following composition: Fragment 1: Ala, Arg, Glu, Met, Phe, Ser Fragment 2: Gly, Lys, Tyr Chymotrypsin digestion yielded three fragments with the listed compositions: Fragment 1: Ala, Gly, Lys, Phe Fragment 3: Arg, Glu, Met, Ser Cyanogen Bromide cleavage yielded two fragments...
Asp-Tyr-Phe-Glu-Asn-Cys-Pro-Lys-Gly The optical absorbance of the peptide at 280 nm is the result of the absorbance of its aromatic amino acids. What is the molar extinction coefficient of vasopressin (ε280) if the molar extinction coefficient of Tyr is 1.2 x 103, and that of Phe is 1.1 x 102?
Consider the following amino acid sequence, found as part of a larger protein: Pro-Gly-Asp-Val-Gln-Phe-Asp-Ile-Arg-Ala-Asp-Gly What kind of structure do you expect this peptide segment be a part of? Where on the protein is this likely to occur?
An octapeptide contains the following amino acids: Met, Thr, Cys, Asp, Phe, Arg, Glu, Gln. Carboxypeptidase treatment of the octapeptide forms Asp and a heptapeptide. Treatment of the octapeptide with Chymotrypsin forms forms two tetrapeptides, A and B. Treatment of A with Trypsin yields two dipeptides, C and D. Edman degradation cleaves the following amino acids from each peptide: Cys (octapeptide), Cys (A), Gln (B), Cys (C), Glu(D). Partial hydrolysis of tetrapeptide B forms Gln-Thr in addition to other products....