Sangers reagent determines the amino terminal aminoacid in the peptide sequence. Sanger's reaction gave cysteine and glutamate. Chymotrypsin digestion provides 3 different fragments. So, the sequence of peptide is,
NH2 - CAHQFLREGDNCDW - COOH
The peptide has 2 positive (histidine and arginine) amino acids. It also has 3 negative (2 aspartate and 1 glutamate) amino acids. So, the net charge on protein sequence is -1.
Please be clear with how you determined the code sequence and isoelectric point 7. A single...
7. A peptide was isolated from sheep hypothalamus and subjected to sequence analysis. The experimental data are as follows. Deduce the amino acid sequence from this data. a. Composition (2Ala, 2Gly, Thr, Phe, Lys, His, Ser, Trp, Arg, Val) b. Reaction of dinitrofluorobenzene with the intact peptide yielded DNP-Thr. A brief treatment with carboxypeptidase a yielded glycine. c. Trypsin digestion yielded three fragments: i. Phe, Thr, Ala, Lys ii. Gly, Val iii. Trp, His, Ser, Gly, Arg, Ala Treatment of...
6. The sequence of kassinin, a tachykinin dodecapeptide from the African frog Kassina senegalensis, was determined. A single round of Edman degradation identifies Asp as the N-terminus. A second sample of the peptide is treated with chymotrypsin. Two fragments are released with the following amino acid compositions: fragment I (Gly, Leu, Met, Val) and fragment II (Asp2, Gln, Lys, Phe, Pro, Ser, Val). Next, a third sample of peptide is treated with trypsin, which results in two fragments with the...
Please explain each part !! Thank you !! #3. Under experimental conditions, you purify a known, biologically important peptide from human tissue. To determine the overall sequence, you then digest the pure peptide with trypsin and chymotrypsin (each separately) and then use mass spectrometry to identify the following sequence fragments from the overall peptide (shown in order of relative length, not necessarily in the order in which they are assembled in the whole, natural peptide). Trypsin cleavage products: Chymotrypsin cleavage...
Explain this question please! Name (4 ofer to the Table of Amino Acids at the beginning of the exam to help solve this problem. Polypeptide I is a 12-mer and has the following amino acid composition: Ala, Arg, 2 His, Leu, 2 Lys, 2 Phe, Ser, Thr, Trp Edman degradation of I shows that its N-terminal amino acid is His. Chymotrypsin cleavage of I yields peptide fragments A-D.Trypsin cleavage of I gives peptide fragments E-G. Shown below is the amino...
please explain how to solve this problem, the answer is provided 9. Peptides: (20 pts.). A polypeptide (X) gives 7 fragments when treated with chymotrypsin (A-G). The same peptide also gives 9 fragments when treated with trypsin (I- IX). After Chymotrypsin A) Thr-Thr-Tyr-Ala-Gly-Phe-Phe-Ile-Asp- Lys B) Ala-Cys-Pro-Leu-Tyr-Gin-lle-Arg C) Met-Ser-Thr-Tyr-Pro-Gly-Arg D) Cys-Leu-Val-Phe-Ile-Lys E) Leu-Ala-Trp-Gly-Val F) Ser-Phe-Ala-Pro-Lys G) Met-Asp-Lys Afier Trypsin I) Ala-Pro-Lys-Met-Asp-Lys-Thr-Thr-Tyr II) Pro-Gly-Arg-Cys-Leu-Val-Phe III) Ile-Lys-Ala-Cys-Pro-Leu-Tyr IV) Ile-Asp-Lys-Met-Ser-Thr-Tyr V) Gin-Ile-Arg-Leu-Ala-Trp VIAla-Gly-Phe VII) Gly-Val VIII) Ser-Phe LX) Phe A) What is the primary...