(a)Draw Histidine in all its protonated form and include the pKa's where appropriate. (b) Calculate the fraction of histidine that has its imidazole side chain protonated at pH7.3. The pKa values for histidine are pK1 = 1.8, pKr (imidazole) = 6.0, and pK2 = 9.2 %3D
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- Oxytocin, a nonapeptide hormone secreted by the pituitary gland, functions by stimulating uterine contraction and lactation during childbirth. Its sequence was determined from the following evidence: 1. Oxytocin is a cyclic compound containing a disulfide bridge between two cysteine residues. 2. When the disulfide bridge is reduced, oxytocin has the constitution Asn, Cys2, Gln, Gly, Ile, Leu, Pro, Tyr. 3. Partial hydrolysis of reduced oxytocin yields seven fragments: Asp-Cys, Ile-Glu, Cys-Tyr, Leu-Gly, Tyr-Ile-Glu, Glu-Asp-Cys, and Cys-Pro-Leu. 4. Gly is the C-terminal group. 5. Both Glu and Asp are present as their side-chain amides (Gln and Asn) rather than as free side-chain acids. What is the amino acid sequence of reduced oxytocin? What is the structure of oxytocin itself?1. Taking the structure of the amino acids into account, give a comparative discussion pK values where histidine=2 and alanine=2.In the case of serine, threonine and tyrosine they have the -OH group in their residue. I'm wondering even though all of them has the -OH groups in their residue. but only the tyrosine has the pKa value with the -OH grouup.
- Taking the structure of the amino acids into account, give a comparative discussion of these pK values : Alanine : 2.34 : 6.1 : 9.70 Histidine: 1.82 : 9.17Determine 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, SerDetermine 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, Met
- The pK value for N1 of adenine is 3.64, whereas the pK value for N1 of guanine is 9.50. Explain this diff erence.Give typed solution only Which of the amino acids shown represents the structure of Ile at pH 10?Why is peptide synthesis carried out from C terminus to N terminus using dicyclohexylcarbodiimide (DCC)? Can you illustrate the explanation with a mechanism/drawing?
- An unknown decapeptide was isolated and characterized. Complete hydrolysis of this peptide gave : F(2), A,G,C,K,N,T, W and V. Treatment with carboxypeptidase releases A. Reaction with Edman’s reagent gave PTH-T and a nonapeptide. The nonapeptide was treated with trypsin and gave 2 peptides: (V-C-G-A) and (N-FF-W-K). Give the sequence of amino acid in the decapeptide.Given the following peptide SEPIMAPVEYPK(a) Estimate the net charge at pH 7 and at pH 12. Assume the pKa valuesgiven in as shown. (b) How many peptides would result if this peptide were treated with(1) cyanogen bromide, (2) trypsin, or (3) chymotrypsin?(c) Suggest a method for separating the peptides produced by chymotrypsintreatment.Glycine has pKa values of 2.34 and 9.60. At what pH does glycine exist in the indicated form?