For the peptide: His-Met-Asp-Tyr-Phe-Ser how many ionizable groups exist?
For the peptide: His-Met-Asp-Tyr-Phe-Ser how many ionizable groups exist?
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
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
Sketch the structure of the tetrapeptide Ser-Phe-Asp-Lys. Clearly show the R groups, all the peptide bonds, the peptide planes, the N-terminus, the C-terminus, and approximate charges on all ionic groups at a pH of 7.0.
3) Chymotrypsin acts on the following pentapeptide: Asp-Lys-Tyr-Gly-Ser. Which portion of the peptide will be the first to leave the enzyme? A) Asp-Lys B Tyr-Gly-Ser C) Asp-Lys-Tyr D Gly-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,...
On your internship, you visit the Mass Spectrometry Lab. Mass spectrometry can identify short peptide fragments based on their molecular weights. Your fellow intern Jerry has neglected to label his tubes of amyloid beta peptide 42 after digesting them with some proteases that we learned about in Module 6: pepsin, trypsin, and chymotrypsin. Help him figure out what protease is in each tube. Jerry’s supervisor has the fragments listed in the same order as the original peptide primary sequence, which...
How many amino acids are there in the disease causing variant of the Amyloid-beta (Ab) peptide? Determine which of these four peptides is most likely to become a beta sheet. Lys-Thr-Val-Ile-Trp-Pro-Phe-Tyr-Ile-Gln-Ile-Gly Arg-Ser-Tyr-Glu-Gly-Leu-Lys-Arg-Ile-Ala-Glu-Ser Ala-Glu-Met-Leu-Gln-Lys-Arg-Gly-Cys-Gly-Asp-Glu Met-Leu-Lys-Ala-Ser-Ala-Leu-Glu-Lys-Leu-Ser-Glu
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?
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,...