Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Draw Glu-His-Trp-Ser-Gly-Leu-Arg-Pro-Gly peptide. What is the net charge of this peptide at pH 3, 8 and 11? What can you say about pI value of this peptide?
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- A) Can you please tell me which of these A.A have a negative side chain? Names of choices in picture provided. B) Can you please tell me which A.A have a hydrophobic side chain and why? Names and choices in picture provided. Thank You so much!!arrow_forward0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.arrow_forwardis it true that aplha and beta are made up of same amino acids but Beta chain is longer than alpha chain?what is other difference and similarity?is the amino aicd sequence exactly the same as well?are their structure the same ?arrow_forward
- Among these amino acid combinations listed above, only the combination of Lys and Glu have side chains with groups that have the greatest ability to stabilize the tertiary structure of a protein. Explain by drawing (a) why Lys and Glu side chain interaction stabilizes the tertiary structure of a protein (b) why the pairs of Glu and Asp & Arg and Pro cannot provide the stability to the protein structure.arrow_forwardBased on the following image, what is the N-terminal AA residue, C-terminal AA residue? What is also the sequence of peptide 2 and peptide 3? Also identify the overall amino acid sequencearrow_forwardDraw the tetrapeptide Met-Ile-Lys-Glu at a ph of 7?arrow_forward
- Polylysine adopts a random structure in solution at physiological pH (i.e. 7.4). Given that the e-amino group of lysine has a pKa of 10.5, under what circumstances do you think polylysine will form an a-helix? Give an explanation for your decision. Given the pKa of the side-chain COOH group, under what circumstances would you anticipate polyglutamate to form an a-helix?arrow_forwardyou have the following peptide Arg-Ile-Pro-Leu-Asp-Lys-Glu The net charge on this peptide at pH 7.0 is ?. The net charge on this peptide at 1M HCl is ?.arrow_forwardConsider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.arrow_forward
- What fragments can be generated in the decapeptide Gly-Lys-Ala-Met-Gly-Gly-Phe-Tyr-Trp-Ala if is subjected to: (a) trypsin, (b) chymotrypsin, and (c) cyanogen bromide.arrow_forward1) Indicate the total charge of the peptide at pH 7.0, 9.0, and 11.0 2) Determine the isoelectric point (pI) for this peptide. Show the relevant pKa’s and your calculation. 3) What is the fraction of the peptide that has the N-terminal amino group deprotonated at pH 9.arrow_forwardIdentify the structure of the predominant form of the pentapeptide at pH = 12 if there is a pentapeptide Ile-Lys-Asp-Phe-Glyarrow_forward
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