3) Chymotrypsin acts on the following pentapeptide: Asp-Lys-Tyr-Gly-Ser. Which portion of the peptide will be the...
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 sequence is more soluble on water. a. Glu-Lys-Leu-Met-His b. Lys-Ser-Ser-Tyr-Glu c. Asp-Phe-Trp-Met-His d. His-Tyr-Ser-Ala-Glu e. His-Ala-Cys-Gly-Glu o
A peptide with the sequence "Glu-Ser-Arg-Asp-Lys" will be cut next to "Arg" by: chymotrypsin elastase trypsin D. All of the above. E None of the above.
Styles A decapeptide has the following amina acid composition: Arg. Asp, Gly, Leu, Lys, Met, Phe, Ser. Trp, and Val Reacting the native peptide with FDNB and then hydrolyzing released 2.4- dinitrophenylvaline. Brief incubation of the native peptide with carboxypeptidase yielded free Leu. Incubation with cyanogen bromide yielded two fragments: a tetrapeptide with composition Met, Phe, Ser, and Val, and a hexapeptide. The hexapeptide yielded 2.4- dinitrophenylglycine. Proteolytic cleavage by trypsin of the native peptide gave free Leu, a tripeptide,...
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
How to do this problem? 1.A 14 AA peptide contains: Ala, Arg,, Gly, His, Leu, Lys, Phez, Serz, Trp, Tyr, Val This peptide yields the following results when broken down into smaller fragments Please note the AA are given in alphabetical order). Show your work, explain your reasoning, give the answer in three letter abbreviation and one letter abbreviation Fragment Content His Treatment Edman Chymotrypsin Gly. His, Phe Ser, Tyr Arg2, Leu, Lys, Ser.Ala, Phe Trp, Val Gly, His, Lys,...
In the octapeptide, Phe-Ile-Ser-Asp-Gly-Haus-Gly-Tyr, which is the C-terminal amino acid? A) Ser B) Phe C) Tyr D) His E) Gly D) Which molecule is an a-amino acid? A) CH CH3CH2CHCHCOZH NH CH CH2CH2CHCHCONH, CH, ICHCONH B) E) CH, CHYCH,CHCHCO,H CN CH, CH3CH2CHCHNH2 NH2 C) CH CH, CH2CHCHCO,H NH
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,...
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?
Calculate the pI for this peptide. Gly Asp Lys Cys Glu His Met Table 1. Group pka c-teminus 3.5 his 6.0 n-terminus 9.0 lys 10.5 asp/glu 4.0 cys 8.4 tyr 10.5 arg 12.5