(a)
Interpretation:
The reason as to why the two protecting groups used for lysine in the synthesis of the peptide
Concept introduction:
Solid-phase peptide synthesis is a technique that is used for peptide synthesis. The peptide is synthesis from C-terminal to N-terminal. It is reverse in biological cells. In this amino protected amino acid is bound covalently on solid phase material with an ester or amide linkage. Then it is deprotected and reacts with another amino protected amino acid. This cycle continues until the desired peptide is not obtained.
(b)
Interpretation:
The structure of each compound obtained from the coupling and decoupling of resin-bound peptide with their explanation is to be stated.
Concept introduction:
Solid-phase peptide synthesis is a technique that is used for peptide synthesis. The peptide is synthesis from C-terminal to N-terminal. It is reverse in biological cells. In this amino protected amino acid is bound covalently on solid phase material with an ester or amide linkage. Then it is deprotected and reacts with another amino protected amino acid. This cycle continues until the desired peptide is not obtained.
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EBK ORGANIC CHEMISTRY
- Determine the amino acid sequence of a polypeptide from the following data: Complete hydrolysis of the peptide yields Ala, Arg, Gly, 2 Lys, Met, Phe, Pro, 2 Ser, Tyr, and Val. Treatment with Edman’s reagent releases PTH-Val. Carboxypeptidase A releases Ala. Treatment with cyanogen bromide yields the following two peptides: 1. Ala, 2 Lys, Phe, Pro, Ser, Tyr 2. Arg, Gly, Met, Ser, Val Treatment with trypsin yields the following three peptides: 1. Gly, Lys, Met, Tyr 2. Ala, Lys, Phe, Pro, Ser 3. Arg, Ser, Val Treatment with chymotrypsin yields the following three peptides: 1. 2 Lys, Phe, Pro 2. Arg, Gly, Met, Ser, Tyr, Val 3. Ala, Serarrow_forwardDetermine the amino acid sequence of a polypeptide from the following data: Acid-catalyzed hydrolysis gives Ala, Arg, His, 2 Lys, Leu, 2 Met, Pro, 2 Ser, Thr, and Val. Carboxypeptidase A releases Val. Edman’s reagent releases PTH-Leu. Treatment with cyanogen bromide gives three peptides with the following amino acid compositions: 1. His, Lys, Met, Pro, Ser 2. Thr, Val 3. Ala, Arg, Leu, Lys, Met, Ser Trypsin-catalyzed hydrolysis gives three peptides and a single amino acid: 1. Arg, Leu, Ser 2. Met, Pro, Ser, Thr, Val 3. Lys 4. Ala, His, Lys, Metarrow_forwardindicate the RIGHT alternative: (a) The Zwitterion form of an amino acid exists only at a point pH value. (b) In a peptide bond there is free rotation at the C-N bond. (c) In a polypeptide, the terminal carboxyl group may be present in its amide form. (d) At a pH greater than pI, an amino acid tends to move towards the cathode in an electrophoresis. (e) At any pH below pI, the predominant form of an amino acid is negatively charged.arrow_forward
- Determine the amino acid sequence of a polypeptide from the following data: Complete hydrolysis of the peptide yields Arg, 2 Gly, Ile, 3 Leu, 2 Lys, 2 Met, 2 Phe, Pro, Ser, 2 Tyr, and Val. Treatment with Edman’s reagent releases PTH-Gly. Carboxypeptidase A releases Phe. Treatment with cyanogen bromide yields the following three peptides: 1. Gly-Leu-Tyr-Phe-Lys-Ser-Met 2. Gly-Leu-Tyr-Lys-Val-Ile-Arg-Met 3. Leu-Pro-Phe Treatment with trypsin yields the following four peptides: 1. Gly-Leu-Tyr-Phe-Lys 3. Val-Ile-Arg 2. Ser-Met-Gly-Leu-Tyr-Lys 4. Met-Leu-Pro-Phearrow_forwardDetermine the amino acid sequence of a polypeptide from the following data:Complete hydrolysis of the peptide yields Arg, 2 Gly, Ile, 3 Leu, 2 Lys, 2 Met, 2 Phe, Pro, Ser, 2 Tyr, and Val.Treatment with Edman’s reagent releases PTH-Gly.Carboxypeptidase A releases Phe. Treatment with cyanogen bromide yields the following three peptides:1. Gly-Leu-Tyr-Phe-Lys-Ser-Met 2. Gly-Leu-Tyr-Lys-Val-Ile-Arg-Met 3. Leu-Pro-Phearrow_forwardDetermine the primary structure of an octapeptide from the following data: Acid-catalyzed hydrolysis gives 2 Arg, Leu, Lys, Met, Phe, Ser, and Tyr. Carboxypeptidase A releases Ser. Edman’s reagent releases Leu. Treatment with cyanogen bromide forms two peptides with the following amino acid compositions: 1. Arg, Phe, Ser 2. Arg, Leu, Lys, Met, Tyr Trypsin-catalyzed hydrolysis forms the following two amino acids and two peptides: 1. Arg 2. Ser 3. Arg, Met, Phe 4. Leu, Lys, Tyrarrow_forward
- Draw a structure for a peptide that gives Gly, Ile & Phe on hydrolysis and fails to react with phenyl isothiocyanate. Mass spectrometry gives a molar mass of 317 for this peptide. Draw the predominant structure at pH 7 using the charge tools to adjust formal charges.arrow_forwardT11.1. A student was provided with the following compounds: (i) N-acetyl-L-Aspartic acid (ii) tert-butyl amine and (iii) coupling agent N,N'-dicyclohexylcarbodiimide (DCC) – to create peptide(s). The synthesis was successfully completed at 100% conversion, where a 2:1 ratio of the amine to amino acid was used and all possible peptide bonds were formed. If partial racemization also took place during the synthesis, how many types of product(s) can the student possibly obtain from the reaction? HO. CH, OH Ö HN. CH, H,C NH2 (A) 1 (B) 2 (C) 3 (D) 4 (E) 5 (F) 6 (G) None of these T11.2. Referring to T11.1: assuming the synthesis was successfully completed at 100% conversion ONLY to form Dipeptide(s) while partial racemization also took place, how many types of Dipeptide product(s) can the student possibly obtain from the reaction? (A) 1 (B) 2 (C) 3 (D) 4 (E) 5 (F) 6 (G) None of thesearrow_forwardCalculate the pl of arginine. Give your answer to two decimal places. pI =arrow_forward
- macollege.instructure.com/courses/352/pages/covid-proteins-lab-manual?module_item_id=D44333 A = abc Where "A" is absorbance, "a" is molar absorptivity, "b" is the path length (length of the cuvette in units of cm), and "c" is concentration (mol/L). The molar absorptivity is an intrinsic property of a molecule which tells us how intensely it will absorb at a particular wavelength. If "A" is a unitless quantity, "b" is in units of cm, and "c" is in units of mol/L, then what are the units of molar absorptivity? Do a little research to learn how alpha-helices and beta-sheets are drawn in protein structures. If most of the absorption properties are coming from the alpha-helices in these proteins, and many alpha-helices have similar absorbance properties across different proteins, which protein would you predict would have the highest molar absorptivity? Your job is to use the following data table to determine the molar absorptivity for each of the following proteins at their respective…arrow_forwardDetermine the amino acid sequence of a polypeptide from the following data:Acid-catalyzed hydrolysis gives Ala, Arg, His, 2 Lys, Leu, 2 Met, Pro, 2 Ser, Thr, and Val.Carboxypeptidase A releases Val.Edman’s reagent releases PTH-Leu.Trypsin-catalyzed hydrolysis gives three peptides and a single amino acid:1. Arg, Leu, Ser 3. Lys2. Met, Pro, Ser, Thr, Val 4. Ala, His, Lys, Metarrow_forward1. Taking the structure of the amino acids into account, give a comparative discussion pK values where histidine=2 and alanine=2.arrow_forward
- Organic ChemistryChemistryISBN:9781305580350Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. FootePublisher:Cengage Learning