Draw the peptide ASK(ala-ser-lysine) with proper stereochemistry? what is its pI(isoelectric point)and why the structure is planar?
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Draw the peptide ASK(ala-ser-lysine) with proper stereochemistry? what is its pI(isoelectric point)and why the structure is planar? Use the following table to look at pka's of the amino acids and solve this question.
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- What amino acid/s is/are isolated when Ala-Lys-Val-Phe—His-Tyr-Gly is treated with trypsin and products are treated further with chemotrypsin? Construct the primary structure of the remaining undigested proteinsTABLE 5.1 Properties of the common amino acids found in proteins pKa of lonizing Residue Mass Occurrence pKa of a-COOH Group a-NH3 Group pKa of Abbreviations 1- and 3-letter codes Name " Side Chaina (daltons) in Proteins (mol %) Alanine A, Ala 2.3 9.7 71.08 8.7 Arginine R, Arg 2.2 9.0 12.5 156.20 5.0. Asparagine N, Asn 2.0 8.8 114.11 4.2 Aspartic acid D, Asp 2.1 9.8 3.9 115.09 5.9 Cysteine C, Cys 1.8 10.8 8.3 103.14 1.3 Glutamine Q, Gln 2.2 9.1 128.14 3.7 Glutamic acid E, Glu 2.2 9.7 4.2 129.12 6.6 Glycine G, Gly 2.3 9.6 57.06 7.9 | Histidine Н, His 1.8 9.2 6.0 137.15 2.4 Isoleucine I, lle 2.4 9.7 113.17 5.5 Leucine L, Leu 2.4 9.6 113.17 8.9 | Lysine K, Lys 2.2 9.0 10.0 128.18 5.5 Methionine М, Met 2.3 9.2 131.21 2.0 Phenylalanine F, Phe 1.8 9.1 147.18 4.0 Proline P, Pro 2.0 10.6 97.12 4.7 Serine S, Ser 2.2 9.2 87.08 5.8 T, Thr W, Trp Y, Tyr Threonine 2.6 10.4 101.11 5.6 Tryptophan 2.4 9.4 186.21 1.5 Tyrosine 2.2 9.1 10.1 163.18 3.5 Valine V, Val 2.3 9.6 99.14 7.2 | Approximate valuoc…Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU I NEED IT ASAP PLEASE
- 0ミレーNレ NH geometry on both cand N. Torigonal plannes CH - C-N o=), HN CH2 CH-C-OH (a- carbon) CH2 HooC Aspaxagine - Toline - Valine - Arginine - phenylalcmine - Glutamic ocid. 1.Give the name and three letter code for each amino acid in the peptide. e 2. At pH 7, approximately what charge would be on your peptide? Explain your answer. 3. Can your peptide form intra/interchain disulfide bonds? Explain why/why not. e 4. Will your peptide absorb UV and is it fluorescent? Explain why/why not. e 5. What is the probability that your peptide contains a cis peptide bond? Explain your answer.Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?Calculate the net charge of the following peptide at pH 2, pH 6 and pH 14 (use 2 and 9 as pKa values for the carboxylic acid and amino groups, respectively, use the attached table for the side chain pKa values). Ile-Leu-Ile-Lys-Glu-Cys-His-Glu-Met-Ile-Ser-Thr-Arg-Tyr
- Based on the pK, table for amino acids (Table 1.1), draw the structures with net charge, and the equilibria representing the complete deprotonation of aspartate. Table 1.1 Name pK pk2 pKR Glycine Alanine 2.4 9.8 2.3 9.7 Valine 2.3 2.4 9.6 Leucine 9.6 Isoleucine 2.4 9.7 Methionine 2.3 9.2 Phenylalanine Proline Serine 1.8 9.1 2.0 10.6 2.1 9.2 Threonine 2.6 10.4 Cysteine Asparagine Glutamine 1.8 10.8 8.3 2.0 8.8 2.2 9.1 Tyrosine Tryptophan Aspartate Glutamate 2.2 9.1 10.9 2.4 9.4 2.0 2.2 10.0 3.9 9.7 4.3 Histidine 1.8 9.2 6.0 10.8 Lysine Arginine 2.2 9.2 1.8 9.0 12.5Of the 20 protein-derived amino acids shown in Table 27.1, which contain Q.) no chiral centerPorcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln 8. How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. 9. List down the different fragments that would result if dynorphin were cleaved by trypsin. 10. How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. 12. Cyanogen bromide is a chemical reagent which also cleaves peptide bonds.…
- After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride, trypsin will cleave the polypeptide only on the C-side of arginine.) Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp In what order will the fragments be eluted from an anion-exchange column using a buffer of pH = 5?The tripeptide +H3N-Leu-His-Glu-COO- has pKa values of 2.2, 3.6, 6.0 and 9.1. The isoelectric point (pI) for this peptide will be: 8 5 6 4 None of the aboveThe melanocyte-stimulating peptide hormone a-melanotropin has the following sequence:Ser–Tyr–Ser–Met–Glu–His–Phe–Arg–Trp–Gly–Lys–Pro–Val(a) Write the sequence using the one-letter abbreviations.(b) Calculate the molecular weight of a-melanotropin, using data inTable