4)a) Draw the peptide ASYTL at pH 7 and 12.b) Draw a Titration Curve for this peptide.c) If this protein were separated by isoelectric focusing, at what pH would youexpect to find it?d) Alcohols usually don't behave as a weak acids, but tyrosine does. Explain why Yionizes, while S and T do not.e) Is Y ionization physiologically relevant? Explain.f)Y is capable of being phosphorylated by kinases in vivo. What mutation mightyou introduce to render Y unphosphorylatable? Constitutively phosphorylated?

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Answered: 4) a) Draw the peptide ASYTL at pH 7…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Consider 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.
Consider the following peptide: Lys-Tyr-Glu-His-Arg-Ala-Asp-Arg-Glu-Tyr-Lys a) What is the net charge of this peptide at pH=1? Show your work. b) What is the net charge of this peptide at pH=14? Show your work.
You have isolated the following peptide: His-Ser-Arg-Ala-Glu-Leu-Pro-Gly A) Calculate the approximate charge of this peptide at pH 1, pH 3, pH 5, pH8, pH 11, and pH 14. B) What is the PI of this peptide?
Given the peptide Lys-Glu-Trp a) Draw the appropriate titration curve for this peptide. Label X and Y axis b) On the graph use X to mark point at which peptide have 0 net charge and Y to mark point where peptide have positive 1 net charge
5a) Draw this peptide at the physiological pH (7.4) with the following 1-letter codes: F-R-I-D-A-Y b) What is its net overall charge? c) Show resonance structures for the protonated version of Arginine's side chain.
In your laboratory, you plan to use ion exchange chromatography to separate the peptide show below from a mixture of different peptides at pH 7.0. Peptide: GDVRWKKFQR A) Draw the structure of the peptide shown above at pH 7. B) Determine the charge of the peptide at pH 7. C) Should you choose a matrix containing DEAE(anion exchange) or CM (cation exchange)? Explain your reasoning in 3-5 sentences. SUBMIT A SINGLE DOCUMENT (PDF) WITH THE THREE REQUIRED ANSWERS. Upload Choose a File
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Consider a peptide with the sequence Ala-Glu-Arg-Leu. Assume the ionizable groups have the pKa values listed in Table 2.1 of your text. (a) Draw the predominant ionic form of the peptide at pH 7.4. (b) Determine the net charge of the predominant form of the peptide at pH 7.4. (c) Calculate the pI of the peptide.
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An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.
Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ? (Select all that apply.) The two peptides have different compositions. The two peptides have different isoelectric points. The two peptides have different titration curves. The two peptides differ in amino acid sequence. [References] If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the y-carbon were replaced by another amino group, what would be the predominant form of this amino acid at pH 12 if the pK, value were 10 for the unique amino group? (Select all that apply.) Both of the carboxyl groups are deprotonated. The amino acid-carries a negative 2 charge. The amino acid carries a negative 4 charge. The amino groups are in the form -NH". Both of the amino groups are deprotonated.
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4) a) Draw the peptide ASYTL at pH 7 and 12. b) Draw a Titration Curve for this peptide. c) If this protein were separated by isoelectric focusing, at what pH would you expect to find it?