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Concept explainers
(a)
Interpretation: A condensed structural formula for the peptide, threonylserine has to be drawn.
Concept introduction: In the IUPAC naming of a peptide, full name is written for the amino acid which is present on the far right. The other amino acid residues in the peptide receive “shortened” names that end in –yl. The –ine or –ic acid ending of the amino acid names is replaced by –yl.
(b)
Interpretation: A condensed structural formula for the peptide, valylglycylcysteine has to be drawn.
Concept introduction: In the IUPAC naming of a peptide, full name is written for the amino acid which is present on the far right. The other amino acid residues in the peptide receive “shortened” names that end in –yl. The –ine or –ic acid ending of the amino acid names is replaced by –yl.
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Chapter 20 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- For the following pentapeptides: Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser A. Compute their isoelectric pH (pI). Show full solution. Use standard pKa values. B. Do these peptides with the same amino acid composition have different net charges at pH 7.0? Explain briefly. C. Would you expect the titration curves of the two peptides to differ? Why or Why not?arrow_forwardWrite the structure of the following peptides: 1. glycyl alanine 2. tyrosyl alanyl glycine 3. phenylalanyl tyrosyl seryl histidine 4. valyl glycyl cystein 5. seryl methioninearrow_forwardDraw the structure of the following 1.Alanylaspartylglutamyltryrosin 2. Tetrapeptidearrow_forward
- Write the Structure Activity Relationship (SAR) of Nifedipine ? Please write at your own words.arrow_forwardConstruct the following lipids: a. Alpha-arachido-beta-clupadonolignocerateb. Alpha-stearidono-beta-gadoleonevonatec. Alpha,beta-dimyristocapratearrow_forwardFor the dipeptide Arg–His, find the pI (the pKs are α-amino 9.0, guanidino 12.5, imidazole 6.0, α-carboxylate 2.1).arrow_forward
- Write a balanced equation showing peptide bond formation between threonine and aspartate.arrow_forwardWhat is the complete name of the peptide attached below? Isoleucylglycylisoleucylleucylvalylalanylglutamine Glycylisoleucylglycylisoleucylvalylalanylasparagine Isoleucylglycylisoleucylleucylvalylisoleucylalanylthreonine Glycylisoleucylleucylvalylisoleucylalanylasparagine Considering only the side chains of the amino acids in the molecule shown above, how many can participate in hydrogen bonding with water? 1 3 5 7arrow_forwardthe following peptide is incubated as chymotrypsin: Gly-Val-Phe-Lys-Ala. Present the detailed chemical mechanism by which chymotrypsin hydrolyzes this peptide. Briefly explain each step. Include only the structure of the final products of the reaction.arrow_forward
- Name the compound: 1. Lys-Ile-Met-Val Draw the forms of the amino acid in the solution. 2. Glutamic Acid (4 forms) 3. Lysine (4 forms)arrow_forwardH CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14arrow_forwardWhat peptides are expected to be produced when α-melanotropin is cleaved by (a) trypsin, (b) cyanogen bromide, or (c) thermolysin? (as shown)arrow_forward
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