1. a. Draw the following pentapeptide:lysine-leucine-aspartate-threonine-phenylalanineb. Label the amino and carboxyl terminus of your peptidec. Label each amino acid residue with one and three letter abbreviationsd. Label the alpha carbonse. Label the bonds around which phi and psi rotational angles occurf. Which amino acid in this chain is most likely to be phosphorylated? Which amino acid is mostlikely to be acetylated?

In the drawn pentapeptide, each amino acid is represented by a letter code, and the peptide bond is…

Answered: 1. a. Draw the following pentapeptide:…

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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1. Amino acid analysis of the peptide gave the following residues: Asp Leu Lys Met Phe Tyr. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was C-C-CH2. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys. What is the amino acid sequence for this heptapeptide?
4. a. Give the full names of the amino acids in this peptide. НзN — CH—С-N—CH— С-N—CH—С—О ČH3 H ČH,OH H. CH2 -ОН b. Calculate the isoelectric point (pl) of a peptide with sequence SNARE. Show your work in a table, giving the pKa values of the ionizable groups, pH, and charges. Step marks are counted. Don't need to write “protonated" or “deprotonated".
2. Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show in zig-zag style, from amino to carboxy terminus, with correct stereochemistry a. Draw the predominant form at pH = 2 b. Draw the predominant form at pH = 5 c. Draw the predominant form at pH = 7 d. Draw the predominant form at pH = 12
Draw the oligopeptides' structure and provide the corresponding name for each oligopeptide 1. Dipeptide Ala-His 2. Tripeptide Glu-Pro-Cys Note: First residue is the N-terminal amino acid
Which of the following is incorrect about the peptide Arg-Asp-Cys-Tyr-Gln-Arg-Glu? O a. Its estimated MW is 770 Da b. None; all the other choices are correct OC. At pH 7, it has a net charge of zero O d. At pH 7, it has six charged groups
29. Amino Acid Chemistry: Using the amino acid chart provided..Ala-Lys-Cys & give the isoelectric point for the tripeptide. Table 23.2 The pK, Values of Amino Acids pk, a-COOH a-NH3* Amino acid side chain Alanine 2.34 9.69 2.17 9.04 12.48 Arginine Asparagine 2.02 8.84 3.86 Aspartic acid Cysteine 2.09 9.82 1.92 10.46 8.35 Glutamic acid 2.19 9.67 4.25 Glutamine 2.17 9.13 Glycine 2.34 9.60 1.82 9.17 6.04 Histidine 2.36 9.68 Isoleucine Leucine 2.36 9.60 2.18 $ 95 10.79 Lysine 2.28 9.21 Methionine 16 9.18 Phenylalanine 1.99 10.60 Proline 2.21 9.15 Serine 2.63 9.10 Threonine 2.38 9.39 Tryptophan Tyrosine 9.11 10.07 2.20 2.32 9.62 Valine O something else! 5.14 O 8.65 something else! 5.81 9.02 9.57
Two peptide sequences are shown below.Peptide A: N-term – GDL – C-termPeptide B: N-term – GTL – C-terma. Draw each peptide at physiological pH. Circle each ionizable functional group in your drawing.b. Briefly explain why changing aspartate to threonine changes the number of ionizable functionalgroups in the peptide chain.c. Briefly explain why the functional group found in aspartate’s side chain is ionizable but the functionalgroup found in threonine’s side chain is not.
please see attached
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
In this sequence: Histidine - Alanine - Aspartic acid - Leucine tetrapeptide (show using your model how the water is released). Show the peptide bonds on your figure. See figure 1
Explain why amino acid can increase blood glucose. Write the structure of each of the following peptide at pH7 and identify how many peptide bond in each number. Alanyl-phenylalanine- aspartate- cysteine Threonyl- Isoleucyl-methionyl- leucine Lysyl-alanine -Phenylalanyl-tyrosyl- serine
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).

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