EBK ORGANIC CHEMISTRY
6th Edition
ISBN: 8220103151757
Author: LOUDON
Publisher: MAC HIGHER
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Chapter 27, Problem 27.78AP
Interpretation Introduction
Interpretation:
The structures of peptides
Concept introduction:
Nucleophilic substitution reaction is the reaction in which a nucleophile attacks the electrophilic center and a substituted product is formed. It takes place by the generation of an electrophilic intermediate. An amide bond formed between a carboxyl group present on the side chain of amino acid and the
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Chapter 27 Solutions
EBK ORGANIC CHEMISTRY
Ch. 27 - Prob. 27.1PCh. 27 - Prob. 27.2PCh. 27 - Prob. 27.3PCh. 27 - Prob. 27.4PCh. 27 - Prob. 27.5PCh. 27 - Prob. 27.6PCh. 27 - Prob. 27.8PCh. 27 - Prob. 27.9PCh. 27 - Prob. 27.10PCh. 27 - Prob. 27.11P
Ch. 27 - Prob. 27.12PCh. 27 - Prob. 27.13PCh. 27 - Prob. 27.14PCh. 27 - Prob. 27.15PCh. 27 - Prob. 27.16PCh. 27 - Prob. 27.17PCh. 27 - Prob. 27.18PCh. 27 - Prob. 27.19PCh. 27 - Prob. 27.20PCh. 27 - Prob. 27.21PCh. 27 - Prob. 27.22PCh. 27 - Prob. 27.23PCh. 27 - Prob. 27.24PCh. 27 - Prob. 27.25PCh. 27 - Prob. 27.26PCh. 27 - Prob. 27.27PCh. 27 - Prob. 27.28PCh. 27 - Prob. 27.29PCh. 27 - Prob. 27.30PCh. 27 - Prob. 27.31PCh. 27 - Prob. 27.32PCh. 27 - Prob. 27.33PCh. 27 - Prob. 27.34PCh. 27 - Prob. 27.35PCh. 27 - Prob. 27.36PCh. 27 - Prob. 27.37PCh. 27 - Prob. 27.38PCh. 27 - Prob. 27.39PCh. 27 - Prob. 27.40PCh. 27 - Prob. 27.41PCh. 27 - Prob. 27.42PCh. 27 - Prob. 27.43APCh. 27 - Prob. 27.44APCh. 27 - Prob. 27.45APCh. 27 - Prob. 27.46APCh. 27 - Prob. 27.47APCh. 27 - Prob. 27.48APCh. 27 - Prob. 27.49APCh. 27 - Prob. 27.50APCh. 27 - Prob. 27.51APCh. 27 - Prob. 27.52APCh. 27 - Prob. 27.53APCh. 27 - Prob. 27.54APCh. 27 - Prob. 27.55APCh. 27 - Prob. 27.56APCh. 27 - Prob. 27.57APCh. 27 - Prob. 27.58APCh. 27 - Prob. 27.59APCh. 27 - Prob. 27.60APCh. 27 - Prob. 27.61APCh. 27 - Prob. 27.62APCh. 27 - Prob. 27.63APCh. 27 - Prob. 27.64APCh. 27 - Prob. 27.65APCh. 27 - Prob. 27.66APCh. 27 - Prob. 27.67APCh. 27 - Prob. 27.68APCh. 27 - Prob. 27.69APCh. 27 - Prob. 27.70APCh. 27 - Prob. 27.71APCh. 27 - Prob. 27.72APCh. 27 - Prob. 27.73APCh. 27 - Prob. 27.74APCh. 27 - Prob. 27.75APCh. 27 - Prob. 27.76APCh. 27 - Prob. 27.77APCh. 27 - Prob. 27.78APCh. 27 - Prob. 27.79APCh. 27 - Prob. 27.80APCh. 27 - Prob. 27.81APCh. 27 - Prob. 27.82APCh. 27 - Prob. 27.83AP
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- Assume that some protein molecule, in its folded native state, has one favored conformation. But, when it is denatured, it becomes a “random coil,” with many possible conformations. (a) What must be the sign of DS for the change: native à denatured? (b) How will the contribution of DS for native denatured affect the favorability of the process? What apparent requirement does this impose on DH if proteins are to be stable structures?arrow_forwardGive the amino acid sequence of each peptide using the fragments obtained by partial hydrolysis of the peptide with acid. a. a tetrapeptide that contains Ala, Gly, His, and Tyr, which is hydrolyzed to the dipeptides His-Tyr, Gly-Ala, and Ala-His b. a pentapeptide that contains Glu, Gly, His, Lys, and Phe, which is hydrolyzed to His-Gly-Glu, Gly-Glu-Phe, and Lys-Hisarrow_forwardGive the amino acid sequence of each peptide using the fragments obtained by partial hydrolysis of the peptide with acid. a. a tetrapeptide that contains Ala, Gly, His, and Tyr, which is hydrolyzed to the dipeptides His–Tyr, Gly–Ala, and Ala–His b. a pentapeptide that contains Glu, Gly, His, Lys, and Phe, which is hydrolyzed to His–Gly–Glu, Gly–Glu–Phe, and Lys–Hisarrow_forward
- (a) Redraw the tripeptide in zwitterionic form (b) Explain how ESI-MS can be used to determine which amino acid is in the middle of the sequence.arrow_forwardA compound is known to have a free amino group with a pKa of 8.8, and one other ionizable group with a pKa between 5 and 7. To 100 mL of a 0.2 M solution of this compound at pH 8.2 was added 40 mL of a solution of 0.2 M hydrochloric acid. The pH changed to 6.2. The pKa of the second ionizable group is?arrow_forwardAnswer the following questions on the basis of the free energies of formation at 25°C shown in the table at the top of the next page: (a) Does the peptide bond between alanine and glycine form spontaneously under standard conditions?arrow_forward
- A peptide has the sequence Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly The p?a values for the peptide’s side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side‑chain pKa glutamate 9.609.60 2.342.34 4.254.25 histidine 9.179.17 1.821.82 6.006.00 tryptophan 9.399.39 2.382.38 serine 9.159.15 2.212.21 glycine 9.609.60 2.342.34 leucine 9.609.60 2.362.36 arginine 9.049.04 2.172.17 12.4812.48 proline 10.9610.96 1.991.99 Calculate the net charge of the molecule at pH 11 and estimate the isoelectric point (pI)(pI) for this peptide.arrow_forwardDraw the structure of the peptide ENDQCW. Draw the stereochemistry of the amino acids. Show the ionization state that would be the major form at pH 1. What is the isoelectric point of the peptide?arrow_forwardWhich of the attached amines can be used to resolve a racemic mixture of amino acids?arrow_forward
- Consider a tripeptide (a peptide that's only 3 amino acids long) composed of one molecule each of lysine, leucine, and the hypothetical amino acid lupine (which doesn't actually exist, so don't try to look it up). Lupine has an ionizable side group with a pKa of 6.3. When this tripeptide is dissolved in an aqueous solution at pH 5.0, the net charge on the molecule is +2. Give the charge on the protonated form of the lupine side group, and the charge on the deprotonated form of the lupine side group.arrow_forwardGlycine is a diprotic acid, which can potentially undergo two dissociation reactions, one for the a-amino group (-NH3), and the other for the carboxyl (-COOH) group. Therefore, it has two pKą values. The carboxyl group has a pK₁ of 2.34 and the a-amino group has a pK₂ of 9.60. Glycine can exist in fully deprotonated (NH₂-CH₂-COO-), fully protonated (NH3-CH₂-COOH), or zwitterionic form (NH3-CH₂-COO-). Match the pH values with the corresponding form of glycine that would be present in the highest concentration in a solution of th pH. fully deprotonated form NH,−CH,−COO- pH 11.9 pH 6.0 pH 8.0 fully protonated form NH3-CH₂-COOH pH 1.0 Answer Bank pH 7.0 zwitterionic form NH3-CH₂-COO-arrow_forwardDenaturation of a protein is a physical change, the most readily observable result of which is loss of biological activity. Denaturation stems from changes in secondary, tertiary, and quaternary structure through disruption of noncovalent interactions including hydrogen bonding and hydrophobic interactions. Three common denaturing agents are sodium dodecyl sulfate (SDS), urea, and heat. What kinds of noncovalent interactions might each reagent disrupt?arrow_forward
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