Explain the following observation: At a pH of 7:0, polylysine, which is a peptide in which all residues are lysine, adopts a random coil. At a pH of 12.0 it adopts a helical structure.
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- Refer to following peptide structure: H&N CH3 IZ CH3- CH₂OH IZ OH ZI CH3 CH3. OH IZ OH IZ CH2 CONH2 parce 0 IZ Calculate the net charge of this peptide at pH = 12. OH CH3 What is the identity of the second residue in the peptide shown below? Enter the capitalized single letter abbreviation. 0- Estimate the pl and round to the nearest whole number. Use pKa values provided in lecture.Illustrate the structure of a peptide with the given sequence below at the given conditions. Serine-Threonine-Glutamic Acid-Lysine-Aspartic Acid-Arginine Form with net charge: -1 Form with net charge: +3 Dominant form at pH 76. Would Lys-Glu-Ser have the same pl as Ser-Glu-Lys? Explain. 7. For a protein, how do you think you might estimate the pI? 8. Draw a dipeptide (use R, and R, for the side chain R groups) and the resonance structures of the peptide bond. 9. Recall the geometry about atoms that participate in double bonds or partial double bonds. What atoms form the rigid plane of the peptide bond (which atoms are coplanar)? 10. How do you expect the rigid plane of the peptide bond to impact folding?
- Consider the following peptide: Lys-His-Asp-Glu-Phe-Cys-Ala-Asp-His-Arg What is the net charge of this peptide at pH = 1? What is the net charge of this peptide at pH = 14?You are given 0.5 M solution of the amino acid Arginine. pK1 (α-carboxyl group) = 2.17 pK2 (α- amino group) = 9.03 and pK3 (guanidine group) = 12.48 Determine the pH of the solution if you add 15 mL 0.25 M HCl to 10 mL of the 0.5 M Arginine. Assume that Arginine is in isotonic state. Show all calculationsYou are given 0.5 M solution of the amino acid Arginine. pK1 (α-carboxyl group) = 2.17 pK2 (α- amino group) = 9.03 and pK3 (guanidine group) = 12.48 Determine the pH of the solution if you add 15 mL 0.25 M HCl to 10 mL of the 0.5 M Arginine. Assume that Arginine is in isotonic state. Show all calculations b. Draw the structure of the amino acid at the pH determined in question 1
- A synthetic polypeptid made up of L-glutamic acid residues is in a random coil configuration at pH 7.0 but changes to alpha helical when the pH is lowered to 2.0. Explain this pH-dependent conformational transition.At physiological pH (i.e. 7.4), polylysine assumes a random structure in solution. Given that the pKa for the e-amino group of lysine is 10.5, under what conditions would you expect polylysine to form an a-helix? Explain your reasoning. Under what conditions would you expect polyglutamate to form an a-helix, given that the pKa for the side-chain COOH group is 4.3?Consider a protein in which a negatively charged glutamic acid side chain (pKa = 4.2) makes a salt bridge (ion-ion interaction) with a positively charged histidine side chain (pKa = 6.5). Part A Do you predict that this salt bridge will become stronger, become weaker, or be unaffected as pH increases from pH = 7.2 to pH = 7.8? The salt bridge will become stronger. The salt bridge will become weaker. The salt bridge will be unaffected. Submit Part B Previous Answers Correct At pH = 7.2 the glutamic acid (Glu) side chain will carry a charge of ~ -1 (at 3 pH units above the pKa for Glu, the side chain will be almost fully ionized); whereas the histidine (His) side chain will carry a charge of < +0.5 (at pH = pK₂ the charge on His would be +0.5; since pH = 7.2 is above its pKa, it will carry less (+) charge as it becomes more deprotonated). As the pH increase to 7.8, the charge on Glu will remain ~ -1 and the charge on His will decrease; thus, this salt bridge is predicted to become weaker…
- Consider the following peptide: alanyl-glutamyl-lysyl-cysteyl-asparagine. 1- Write the semi-developed formula of this peptide at pH = 1. Indicate the N- terminal and C-terminal ends of the peptide. Indicate the carbones a. 2- This peptide comprises 5 ionisable groups whose pKa values are, respectively: 2 ; 4.3 ; 8.3 ; 9.7 ; 10.5. Attribute a pKa value to each ionisable group. Justify your answer answer (using the Table, p. 8 when necessary).Draw the structure of the dipeptide Thr-Cys at pH7. Make sure the following are clearly indicated: - the amion terminus (N)- the carboxly terminus (C)- a peptide bond - an alpha-carbon atomYou have isolated from a rare fungus an octapeptide that prevents baldness and you wish to determine its amino acid sequence. The amino acid composition is K2, D, Y, F, G, S, A. Reaction of the intact peptide with dansyl chloride yields dansyl-A. Cleavage with trypsin yields peptides whose compositions are: (K, A, S) and (G, F, K) plus a dipeptide. Reaction with chymotrypsin releases free D, a tetrapeptide with composition (k, S, F, A) and a tripeptide whose composition following acid hydrolysis is (G, K, Y). The enzymatic digests are each carried out on the whole, undansylated peptide.What is the sequence?