b) Consider the following experimental results: Total hydrolysis of a nonapeptide gave: Ala,Arg,Glu,Leu,Lys,Met,Phe,Tyr,Val One fragment from CNBr treatment was: Tyr-Leu-Lys One fragment from Chymotrypsin treatment was Arg-Glu-Met-Tyr One fragment from Trypsin treatment was Val-Ala-Phe-Arg i. Deduce, with suitable explanations, the amino acid sequence of the nonapeptide.
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- b) Consider the following experimental results: Total hydrolysis of a nonapeptide gave: Ala,Arg,Glu,Leu,Lys,Met,Phe,Tyr, Val One fragment from CNBr treatment was: Tyr-Leu-Lys One fragment from Chymotrypsin treatment was Arg-Glu-Met-Tyr One fragment from Trypsin treatment was Val-Ala-Phe-Arg ii. The reagent shown below is widely utilized in the sequencing of peptides. Treatment of the nonapeptide you deduced in part i. with this reagent yields a phenylthiohydantoin derivative, compound 1, and an octapeptide. Write a mechanism for the formation of compound 1. N=c=8Please provide a separation solution of combining two types of chromatography to isolate the protein A from the mixture containing protein A, B, C and D (shown as below). And then explain the related mechanisms in details. Protein A: Met-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu- Protein B: Met-Asp-Glu-Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu Protein C: Met-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu-Val-Val-Val- Ile-lle-lle-Leu-Leu- Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle- lle-Leu-Leu-Leu-Leu-Val-Val-Val-Ile- Protein D: Met-Asp-Glu--Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu-Glu-Asp- Glu-Asp-Glu-Glu-Asp-Asp-Glu-Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu-Glu- Asp-Glu-Asp-Glu-Glu-Asp-Glu-Glu-AspA decapeptide was analyzed and the following information obtained. Determine the primary structure of the peptide. Edman's Degradation: PTH-Ala Trypsin produces 3 peptides of the following composition: 1. Gly, His 2. Ala, Leu, Lys, Val 3. Arg (2), Phe, Pro Chymotrypsin produces 2 peptides of the following composition: 1. Ala, Leu, Lys, Phe, Val 2. Arg (2), Gly, His, Pro Elastase produces 1 amino acids and 3 peptides 1. Ala 2. Leu, Val 3. Arg (2), Lys, Phe, Pro, Gly, His Arg Gly His Leu Phe Pro Val
- A tetrapeptide, glutamate-glycine-alanine-lysine, is prepared at at concentration of 1 mM (0.001 M) and is measured in the standard setup (pathlength of 1 cm). What is the approximate absorbance of this peptide at 280 nm? Hint: if the peptide contained a single tryptophan, the answer would be about 10. 10 280 1 0The peptide Leu-Cys-Arg-Ser-Gln-Met is subjected to Edman degradation. After the first cycle of this process, the products that are generated are: O PTH-Leu, PTH Cys, PTH-Arg. PTH-Ser, PTH-GIn, and PTH-Met O PTH-Leu-Cys-Arg-Ser-Gin-Met O PTH-Met and Leu-Cys-Arg-Ser-Gin-Met O PTH-Leu-Cys and PTH-Arg-Ser-Gin-Met O PTH-Leu and Cys-Arg-Ser-Gln-MetH CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14
- An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate) with serum enzymes (Eadie, 1949). In the experiment, two experiments were conducted, namely experiment 1 without using a prostigmine inhibitor and experiment 2 using a prostigmine inhibitor at 1.5 x 10^-7 mol/l. the data obtained are: a. Is prostigmine competitive or noncompetitive inhibitor? b. determine the value of km and rmax for the two experiments, compareShow the peptides that would result from cleavage by the indicated reagent: a. Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A b. Ser-Phe-Lys-Met-Pro-Ser-Ala-Asp by cyanogen bromide c. Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsinAfter being stabilized with supplemental oxygen, a blood transfusion, and medication to help with the pain, JJ was prescribed the drug hydroxyurea to help increase the level of fetal hemoglobin (ay2) in the red blood cell. Though the exact pharmacological effect of hydroxyurea is unclear in the treatment of Sickle Cell Disease, it is known that the drug is an inhibitor of ribonucleotide reductase and acts to transiently inhibit deoxyribonucleotide synthesis in dividing cells. Q5: In which phase of the cell cycle does hydroxyurea produce its main effect?
- Will rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, IIIGiven the undecapeptide un sequenced Ala2, Arg, Glu, Lys, Met, Phe, Ser, Thr, Trp, Val. Edman Degradation identified Ala. It is further analyzed and degraded to four fragments using trypsin- catalyzed hydrolysis and yielded the following Ala – Glu – Arg ;Thr – Phe – Lys ; Lys ; and Met – Ser – Trp – Val . To further analyze the undecapeptide A.A Sequence, Chymotrypsin -catalyzed hydrolysis identified two fragments Ala – Arg – Glu – Phe – Thr and Lys – Met – Ser – Trp – Val and lastly treatment with cyanogen bromide identified two fragments: Ala – Arg – Glu – Lys – Met – Phe – Thr – Val; and Trp – Ser what is the name of the undecapeptide?Predict the fragments that will be generated from the treatment of the following peptide with: a) trypsin; b) chymotrypsin; c) and S. aureus V8 protease: Gly-Ala-Trp-Arg-Asp-Ala-Lys-Glu-Phe-Gly-Gln