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ORGANIC CHEMISTRY-ETEXT REG ACCESS
12th Edition
ISBN: 9781119308362
Author: Solomons
Publisher: WILEY
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Chapter 24, Problem 21P
Interpretation Introduction
Interpretation:
The structural feature of polyglutamic acid and the chemical change for given transformation are to be explained.
Concept introduction:
The
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The amino acid (S)-alanine has the physical characteristics listed under the structure.
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Chapter 24 Solutions
ORGANIC CHEMISTRY-ETEXT REG ACCESS
Ch. 24 - Prob. 1PPCh. 24 - Practice Problem 24.2 The guanidino group NHNHCNH2...Ch. 24 - Prob. 3PPCh. 24 - Prob. 4PPCh. 24 - Prob. 5PPCh. 24 - Prob. 6PPCh. 24 - Prob. 7PPCh. 24 - Practice Problem 24.8
Glutathione is a tripeptide...Ch. 24 - Prob. 9PPCh. 24 - Prob. 10PP
Ch. 24 - Prob. 11PPCh. 24 - Practice Problem 24.12 Show all steps in the...Ch. 24 - Practice Problem 24.13 The synthesis of a...Ch. 24 - Practice Problem 24.14
The terminal carboxyl...Ch. 24 - Prob. 15PPCh. 24 - Prob. 16PPCh. 24 - (a) Which amino acids in Table 24.1 have more than...Ch. 24 - Prob. 18PCh. 24 - 24.19 (a) On the basis of the following sequence...Ch. 24 - Prob. 20PCh. 24 - Prob. 21PCh. 24 - Prob. 22PCh. 24 - Prob. 23PCh. 24 - Prob. 24PCh. 24 - The enzyme lysozyme and its mechanism are...Ch. 24 - Prob. 2LGP
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- Show the condensation reactions that result in the formation of the tetrapeptide Asp-Gly-Ser- Gln. After you have finished the synthesis change the structure to show how it would exist in a cell at physiological pH (pH = 7).arrow_forward(a) The isoelectric point (pI) of phenylalanine is pH 5.5. Draw the structure of the major form of phenylalanine at pHvalues of 1, 5.5, and 11.(b) The isoelectric point of histidine is pH 7.6. Draw the structures of the major forms of histidine at pH values of 1, 4,7.6, and 11. Explain why the nitrogen in the histidine ring is a weaker base than the a-amino group.(c) The isoelectric point of glutamic acid is pH 3.2. Draw the structures of the major forms of glutamic acid at pH valuesof 1, 3.2, 7, and 11. Explain why the side-chain carboxylic acid is a weaker acid than the acid group next to thea-carbon atomarrow_forwardThe amino acid sequence shown below is a short excerpt (residues 130-172) from the rod domain of an a-keratin-like protein. Predict the effect of each of the amino acid substitutions (stabilize, destabilize, no effect) and explain your reasoning. 130 - ATEFKTRFDDAALRANDIQL VIRSNEITADLIKDRLDQITTYY - 172 a) Substitution of S in place of A at position 140. b) Substitution of V in place of I at position 147.arrow_forward
- For the peptide Ala‑Arg‑Lys‑Ala‑Asn‑Ser‑Ala‑Ser, what would be the expected charges at pH 1, 7,pH 1, 7, and 13?arrow_forwardDraw the structure of the tetrapeptide Asp-Arg-Val-Tyr. Please show the appropriate stereochemistry of the natural amino acids in the resulting peptide. Please draw all ionizable groups in their neutral form.arrow_forwardSuggest a scheme you will follow to synthesise the dipeptide Ala-Glyarrow_forward
- Draw the structure of the predominant form of(a) isoleucine at pH 11.arrow_forwardTaking the structure of the amino acids into account, give a comparative discussion of these pK values : Alanine : 2.34 : 6.1 : 9.70 Histidine: 1.82 : 9.17arrow_forwardThe first step in the catabolism of most amino acids is the removal of the nitrogen atom by transfer to an a-keto acid, a reaction catalyzed by an enzyme called a transaminase. The a-keto acid acceptor is often a-ketoglutarate. Modify the structures in the product to show the products of the transamination of cysteine. Be sure to show functional groups with the charge and number of attached hydrogen atoms appropriate for pH 7.4. transaminase + O=C H₂N-CH + CH₂ CH₂ CH₂ SH Incorrect H₂N || CH | CH₂ | CH₂ I || O || n | CH₂ T SHarrow_forward
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