Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU
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Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU
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- Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEUCut the following protein with the Serine Proteolytic enzyme Trypsin. How many peptide fragments are present after the protein is treated with Trypsin? Ala-Leu-Arg-Gly-Met-Val-Arg-Lys-Ala O 2 6. 8.Consider the following two peptides: I. N-Pro-Pro - Glu - Glu - Tyr - His - Cys - Ala - Glu - Gln - Lys - Leu - Ser - Ser - Phe-Leu- Thr - C II. N-Pro-Pro - Lys - Arg - Gly - Tyr - His - Gly - Glu - Asp - Glu - Asp - Glu - Ser - Gly-Phe- Tyr-C Give three reasons why_peptide I is more likely to form an alpha helix in aqueous solution at pH 7.0. Your reasons may include why_peptide Il is less likely to form an alpha helix
- Draw the structure of this peptide: N-Met-His-Tyr-Leu-Asp-Ser-Arg-Leu-CGiven below are sequences of amino acids present in an oligo-peptide chain. Count the overall chargeof each assigned peptide and write it in your answer. Along with it also mention that toward swhichelectrode (cathode or anode) will the peptide move? Please remember that cathode is a negativeelectrode and anode is a positive electrode. Ile-Lys-Arg-Trp-Lys-Asn-Glu-His-Pro-Asp-Ala-Tyr-Phe-Glu-Met-Phe-Gly-ValPorcine 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.…
- Circle and name two different amino acids in this peptide: Kahalalide F HN HN HO NH HN HNWrite the peptides of the full name " RYJO NNALAMBA" Every symbol of the Fullname writes the expanded structure in a zwitterion form. Then give the name of the polypeptide as a single molecule of the full namefor the following amino acids below circle the r groups then tell me if they are polar or nonpolar
- Name the peptide* O H O H H,'N-CH-C-N-CH-C-N-CH-C-o CH CH, CH; CH-CH, CH, SH CH, O Methionyl-leucynyl-cycteine Methionyl-leucinyl-cycteine Leucyl-methionyl-cycteinyl Methionylleucyl-cysteineIdentify and encircle the peptide bonds in this polypeptide (Asp-Sec-Leu-Cys-Glu).A peptide has the sequence Glu-His-Trp-Ser-Gly-Leu-Arg-Pro-Gly The pK₁ values for the peptide's side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side-chain pKa glutamate 9.60 2.34 4.25 histidine 9.17 1.82 6.00 9.39 2.38 9.15 2.21 9.60 2.34 9.60 2.36 9.04 2.17 10.96 1.99 tryptophan serine glycine leucine arginine proline Calculate the net charge of the molecule at pH 3. Calculate the net charge of the molecule at pH 8. 12.48 net charge at pH 3: net charge at pH 8: