D raw the full structure of the following tetrapeptide . Label the N terminal and C terminal residues. Phe - Cys - Ser - Ile
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D raw the full structure of the following tetrapeptide . Label the N terminal
and C terminal residues.
Phe - Cys - Ser - Ile
Step by step
Solved in 3 steps with 1 images
- From the peptide chain: Met-Tyr-Phe-Arg-Ile-Glu-Asn-Asp-Ser, draw the structure of the product formed when reacted with ElastaseTranslate the following amino acid sequence into one-letter code: Glu-Leu-Val-Ile-Ser-IleSer-Leu-IleVal-Ile-Asn-Gly-Ile-Asn-Leu-Ala-SerValGlu-Gly-Ala-SerConsider 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
- Determine whether each of the amino acids is polar, nonpolar, positively charged, or negatively charged at pH 7. Polar and neutral aspartate H Ser H₂N-C-CH₂-C-COO NH3 lysine Leu Nonpolar Answer Bank H OOC-CH₂-CH₂-C-COO NH3 Positively charged H CH₂-C-COO NH3 hydrophobic amino acids Negatively chargedExamine the peptide. Thr‑Lys‑Pro‑Ile‑Val‑Ala‑Pro‑Met‑Glu‑Tyr‑Gly‑LysThr‑Lys‑Pro‑Ile‑Val‑Ala‑Pro‑Met‑Glu‑Tyr‑Gly‑Lys Write the sequence using one‑letter abbreviations. Estimate the net charge on the peptide at pH 7. Estimate the net charge on the peptide at pH 12.27. Draw palmitic acid, identify a, B and w carbons, write out its short hand notation 28. Examine the peptide sequence below and then answer the questions: H2N-Gly- Leu- Ala-Asp-Cys-Asn-Trp-lle-Ser-Phe-Lys-Cys-Arg-Pro-coOH a. Circle the asparagine residue b. A possible intramolecular disulfide bond can be formed within this peptide between which two residues? c. Circle one residue which has a positively charged side chain under pH 7.4 d. Circle one residue which has a negatively charged side chain under pH 7.4 e. Circle the residue which can be phosphorylated
- Use circles to represent amino acids in the polypeptide shown below. OColor each amino acid using the color scheme: polar, basic amino acid = blue; polar acidic amino acid = red; non-polar amino acid = yellow H3N*-ala-ile-trp-arg-gly-ala-his-tyr-trp-gly-gly-tyr-arg-ile-val-thr-ile-trp-cys- met-gly-ile-asp-cys-thr-glu-cys-trp-gly-cys-phe-arg-his-pro-val-phe-Co-Given this peptide chain:LYS – MET – ASP – THR – GLN – ARG- LYS – TRP – MET – LYS – GLU – VAL- ARGIf the first 5 amino acid residue are subjected to anion exchange chromatography, which amino acids will come NOT out of the column? Please explain.Draw the peptide formed between asparagine and histidine. H,N- -CH-C-OH H,N-CH-ċ-OH ČH2 ČH, N° NH2 -NH +
- The sequence of a peptide is given below. Ala-gly-val-leu-trp-lys-ser-phe-arg-proWhich peptide bond(s) are cleaved by chymotrypsin(A peptide has the sequence Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–GlyGlu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly The p?apKa 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 9.609.60 2.342.34 4.254.25 histidine 9.179.17 1.821.82 6.006.00 tryptophan 9.399.39 2.382.38 serine 9.159.15 2.212.21 glycine 9.609.60 2.342.34 leucine 9.609.60 2.362.36 arginine 9.049.04 2.172.17 12.4812.48 proline 10.9610.96 1.991.99 Calculate the net charge of the molecule at pH 3.The dynorphins are a group of opioid peptides that play an important role in changes in the brain associated with cocaine addiction. One of these peptides, dynorphin A, contains the following amino acid sequence: Tyr–Gly–Gly–Phe–Leu–Arg–Arg–Ile–Arg–Pro–Lys–Leu–Lys. Draw the amino acids and peptide fragments formed when dynorphin A is treated with each reagent or enzyme: (a) chymotrypsin; (b) trypsin; (c) carboxypeptidase; (d) C6H5N=C=S.