Peptide ionization Consider a peptide with the sequence Ser-His-Glu-Cys-Arg-Gln. You will be asked to state the charge on the functional groups of this peptide at pH 1 and pH 9.5. You will also be asked to calculate the net charge on the peptide. You may find it convenient to write down the charge on each group on a piece of paper as you go along, so that you can add them up at the end.
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The net charge of the each amino acid residue in a peptide is determined by the side chain pK of the amino acid, along with the alpha amino and alpha carboxyl group at the N- and C-terminal ends respectively. It is also determined by the pH of the buffer in which the peptide is dissolved.
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- Leu-Trp-Phe-Met-Ala-Ile-Val- Draw the structure of the peptide at pH7.4. and Indicate the hydrogen bonds formed in the alpha helix.His-Met-Asp-Tyr-Phe-Ser Calculate an approximate pI (isoelectric point) for this peptide. Please use the pKa's listed within Table 3-1 of Lehninger. Show and/or explain all your work; you must be very clear about WHY you use particular pKa's in your calculation.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.
- Thr-Lys-Pro-Ile-Val-Ala-Pro-Met-Glu-Tyr-Gly-Lys Write the sequence using one-letter abbreviations. sequence: TLPIVAPMGYGK Incorrect Estimate the net charge on the peptide at pH 7. charge at pH 7: +1 Estimate the net charge on the peptide at pH 12. charge at pH 12: 0 IncorrectPro-Ser-Ala-Phe-Glu. Draw this peptide at pH 7 and include its stereochemistry.peptide Lys-Glu-Trp answer the following questions: Draw the structure of this peptide when all the ionizable groups are fully protonated. How many ionizable groups does this peptide have? Label the pKa for each of the ionizable groups in the structure above. Draw the appropriate titration curve for this peptide on graph paper starting at pH 0 and ending at pH 14. Label the x-axis, y-axis and the pKa Determine the overall net charge of this peptide at each full equivalent point (including 0) where the ionizable group is 100% deprotonated. Determine the pI for this peptide. Determine the average overall net charge of a mixture of this peptide in a solution where pH=8.5.
- draw the peptide structure n-GYSEDAK-c in low pHAla-Arg-Val-His-Asp-Gln Given the polypeptide chain above Estimate the net charge of the polypeptide chain at physiological pH (7.4) and at pH 5.0 . How many peptide bonds are there? What kind of polypeptide is it?Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU I NEED IT ASAP PLEASE
- N- HO sta on e yor current pH the peptide? Explain your yor a) Based the charge state shown, what is a possible vahe amswer wsi'ng 2-3 sentences. Show the qull pH ramge yor this protonation otate 6) Hypo thesize a oingle amino acid substitution Cmutation) that wonld make Your amswer must include the which residue this lic You. peptide more hydrophi you would mutate and what new re sidue would take its place Include a 1 sentence explanation g your reasoning yourPeptide sequence using 1-letter code for amino acids: EDLSMTCFRH What is the net charge of this peptide at pH 9? Use the pKa values from Table 4-1 from Voet, Voet and Pratt. -2 -1 O +1 +2structure of valine at pH of 12