pKas of ionizable groups of amino acids and peptides:Serine (hydroxyl):Threonine (hydroxyl):amino acid carboxyl:amino acid amino:Aspartate (carboxyl): 4Glutamate (carboxyl): 4Histidine (imidazole): 6Cysteine (sulfhydryl): 8.5Tyrosine (hydroxyl):Lysine (amino):10.510.5Arginine (guanadino): 12.5131329.5 Draw the amino acid below in its most protonated form, any intermediately protonatedforms, and its least protonated form.Also draw a titration curve for this amino acid, with pH on the y-axis and equivalents on thex-axis going from acidic to basic (most protonated to least protonated) using the pka valuesbelow.Match the protonated/deprotonated forms to the appropriate regions of the titration curve.Scan your drawing, and upload as a pdf, jpeg, or tiff file.H3CONH₂pKas are provided below:OH

pH = 1/Log [H+] If [H+] concentration in a solution is high, pH will be low and the solution is…

Answered: Draw the amino acid below in its most…

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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Similar questions

Calculate the net charge of the following peptide at pH 2, pH 6 and pH 14 (use 2 and 9 as pKa values for the carboxylic acid and amino groups, respectively, use the attached table for the side chain pKa values). Ile-Leu-Ile-Lys-Glu-Cys-His-Glu-Met-Ile-Ser-Thr-Arg-Tyr
Sketch a titration curve for the following amino acids and indicate the pKa values for all titratable groups. Also indicate the pH at which this amino acid has no net charge. aspartic acid gly-val
For the following pentapeptides: Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser Draw the most protonated forms of the pentapeptides Illustrate the ionization of the pentapeptides from the most protonated to its deprotonated form. Label the ionization with its respective pK values. Compute their isoelectric pH (pI). Do these peptides with the same amino acid composition have different net charges at pH 7.0? Explain briefly. Would you expect the titration curves of the two peptides to differ? Why or Why not?
At which pH would the peptide with the amino acid sequence 'KEYHR' be found in an IPG (Immobilized pH gradient) strip after successful isoelectric focusing. Show calculation. lonizable groups Alpha amine group of K Side chain group of K Side chain group of E Side chain group of Y Side chain group of H Side chain group of R Alpha carboxylic acid group of R pka 8.95 10.53 4.25 10.07 6 12.48 2.17
With regards to arganine illustrate the pH-dependent transitions on a titration graph from most to least protonated. Indicate also the relevant part of the amino acid which is associated with the transition on that part of the graph.
Determine the pI of the peptide H2N-Ala-Lys-Ser-Arg-COOH at pH 11, please explain why some pKas are used in the solution of the problem while others are not.
Experimental results describing a protein's amino acid composition are useful for estimating the molecular weight (MW) of the entire protein. A quantitative amino acid analysis reveals that bovine cytochrome c contains 1% tryptophan (M, 204) by weight. Calculate the approximate molecular weight of bovine cytochrome c if there is 1 tryptophan residue. Please enter your answer with three significant figures. approximate bovine cytochrome c MW: number of threonine residues: 19.4 20.4 x10³ Bovine chymotrypsinogen has a molecular weight of 25.6 kDa. Amino acid analysis shows that this enzyme is 9% threonine (M, 119). Calculate how many threonine residues are present in a molecule of bovine chymotrypsinogen. Round your answer to the nearest whole number. Incorrect Incorrect Da
The pKa for histidine is pKa = 6.1 while that for cysteine is pKa = 8.0 2. Assume that both histidine and cysteine are catalytic groups for a particular enzyme. Assume also that the side chain of cysteine must be in the deprotonated form. Estimate the pH at which the catalytic activity of this enzyme is the maximum and sketch a pH-activity graph.
Some of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.
Solve for the isoelectric point of the following amino acids. Draw the species present before and after each pKa to show the zwitterion of the amino acids. 1. Phenylalanine 2. Glutamic acid
A mixture of Asparagine (pl 5.41), Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2: v First 1. Asparagine v Second 2. Aspartic Acid 3. Histidine v Third 4. Lysine v Fourth 5. Threonine v Fifth 6. No separation
Draw an ionization scheme for each of the amino acids Phenylalanine, Methionine, Tyrosine, Asparagine (from the most acidic form to the most basic form) , and show your computation for the pI/IP of each of the amino acids as well. Draw a complete structural representation for the tetrapeptide Phe-Met-Tyr-Asn (NOTE:use the zwitterion form) Give the IUPAC name for the tetrapeptide formation of F-M-Y-N. List all the possible tetrapeptide formed from one of each amino acids Phe-Met-Tyr-Asn? (NOTE: Use the three letter abbreviation code for the amino acids in answering D)

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