Organic Chemistry
8th Edition
ISBN: 9781305580350
Author: William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote
Publisher: Cengage Learning
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Chapter 23.5, Problem GQ
Interpretation Introduction
Interpretation:
An explanation for the given order of association found in DNA has to be identified from the given options.
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The denaturing of proteins occurs when the stabilizing forces are altered. Below is the set of processes in which proteins are denatured.
Classify the following processes according to the denaturing agent involved.
Please help me understand the diff and correct any mistakes.
Histones are proteins found in eukaryotic cell nuclei. They wrap DNA around itself, thereby compacting the phosphate-rich DNA the nuclei. Histones have a very high pI, usually around 10.8. What amino acid residues must exist in relatively large numbers in Histones? In what way do these residues contribute to the strong binding of Histones to DNA? Where do you expect the majority of these residues to be situated on the histone protein structure?
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.
Chapter 23 Solutions
Organic Chemistry
Ch. 23.1 - Prob. 23.1PCh. 23.2 - Prob. 23.2PCh. 23.2 - Prob. 23.3PCh. 23.2 - Prob. 23.4PCh. 23.5 - Prob. 23.5PCh. 23.5 - Prob. AQCh. 23.5 - What is the hybridization of the nitrogen in...Ch. 23.5 - Prob. CQCh. 23.5 - The pKas of the conjugate acids of aniline and...Ch. 23.5 - Prob. EQ
Ch. 23.5 - Prob. FQCh. 23.5 - Prob. GQCh. 23.5 - Select the stronger acid from each pair of...Ch. 23.6 - Prob. 23.7PCh. 23.6 - Prob. 23.8PCh. 23.6 - Prob. 23.9PCh. 23.7 - Prob. 23.10PCh. 23.8 - Prob. 23.11PCh. 23.8 - Prob. 23.12PCh. 23.8 - Prob. 23.13PCh. 23.9 - Prob. 23.14PCh. 23.10 - In Example 23.15, you considered the product of...Ch. 23 - Prob. 23.16PCh. 23 - Prob. 23.17PCh. 23 - Prob. 23.18PCh. 23 - Prob. 23.19PCh. 23 - Prob. 23.20PCh. 23 - Prob. 23.21PCh. 23 - Prob. 23.22PCh. 23 - Account for the formation of the base peaks in...Ch. 23 - Prob. 23.24PCh. 23 - Select the stronger base from each pair of...Ch. 23 - The pKa, of the conjugate acid of morpholine is...Ch. 23 - Which of the two nitrogens in pyridoxamine (a form...Ch. 23 - Prob. 23.28PCh. 23 - Prob. 23.29PCh. 23 - Prob. 23.30PCh. 23 - Prob. 23.31PCh. 23 - Suppose you have a mixture of these three...Ch. 23 - Prob. 23.33PCh. 23 - Prob. 23.34PCh. 23 - Prob. 23.35PCh. 23 - Prob. 23.36PCh. 23 - Prob. 23.37PCh. 23 - (S)-Glutamic acid is one of the 20 amino acid...Ch. 23 - Prob. 23.39PCh. 23 - Propose a structural formula for the compound...Ch. 23 - Prob. 23.41PCh. 23 - The pyrolysis of acetic esters to give an alkene...Ch. 23 - Propose steps for the following conversions using...Ch. 23 - Show how to bring about each step in this...Ch. 23 - Show how to bring about each step in the following...Ch. 23 - Prob. 23.48PCh. 23 - Prob. 23.49PCh. 23 - Methylparaben is used as a preservative in foods,...Ch. 23 - Prob. 23.51PCh. 23 - Prob. 23.52PCh. 23 - Propose a synthesis for the systemic agricultural...Ch. 23 - Prob. 23.54PCh. 23 - Several diamines are building blocks for the...Ch. 23 - Prob. 23.56PCh. 23 - Prob. 23.57PCh. 23 - Prob. 23.58PCh. 23 - Prob. 23.59PCh. 23 - Following is a retrosynthesis for the coronary...Ch. 23 - Prob. 23.61PCh. 23 - Prob. 23.62PCh. 23 - Given this retrosynthetic analysis, propose a...Ch. 23 - Prob. 23.64PCh. 23 - Following is a series of anorexics (appetite...Ch. 23 - Prob. 23.66PCh. 23 - Prob. 23.67PCh. 23 - Show how the synthetic scheme developed in Problem...Ch. 23 - Prob. 23.69PCh. 23 - Prob. 23.70PCh. 23 - Prob. 23.71PCh. 23 - Prob. 23.72P
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- Although the bond energy for the hydrogen bond in a vacuum is estimated to be about 20 kJ/mol, we find that each hydrogen bond in a folded protein contributes much less--probably less that 5 kJ/mol--to the enthalpy of protein stabilization. Suggest an explanation for this difference. Explain briefly.arrow_forwardExplain why casein precipitates when vinegar is added. Why was milk or raw egg once used as an antidote in cases of heavy metal poisoning? Based on your isolated yield of casein, how many grams of the protein are in one 200 g glass of milk? Which of the solutions contained amide bonds? Which test tells you this? Which of the solutions contained compounds with primary amino groups? Which test tells you this? Describe two examples of protein folding patterns and identify what level of protein structure they belong to. What other reagents might you use besides ferric chloride to test affinity for metal ions?arrow_forwardDescribe two examples of protein folding patterns and identify what level of protein structure they belong to. What other reagents might you use besides ferric chloride to test affinity for metal ions? How many grams of the protein are in one 200 g glass of milk?arrow_forward
- The charge form of the aspartic is believed to participate in a reaction catalyzed by an enzyme. At pH = 9.0, what is the probability that the aspartic acid will be charged?arrow_forwardA peptide has the sequence Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–GlyGlu–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 8arrow_forwardOne of the most advanced methods for determining a protein sequence is tandem mass spectrometry (MS/MS). Select from the list of statements below all that applies to MS/MS. Group of answer choices CID is one way of performing tandem MS experiments The experiment start by chopping the protein into smaller peptide fragments using an enzyme These peptide fragments are later introduced into the mass spectrometer to determine their molecular weight Peptide fragments are selected for further fragmentation by collision with an inert gas There are only 4 types of ions which can result from MS/MS fragmentation: a, b, x, and y ions The a and b ions are the ones with the original C terminus, whereas the x and y ions are the ones with the original N-terminus All of the abovearrow_forward
- 5 ased on molecular weights of purified (no beta-Me) and (beta-Me) sample, which are 97.4 kDa and 47.2 kDa, what can be said about the number and size of the protein monomers, as well as the nature of the bonds holding together the complete quaternary structure of the proteins?arrow_forwardWhat observations led Linus Pauling and his colleaguesto hypothesize that the peptide bond exists as a resonancehybrid?arrow_forwardHow can the Michaelis constant (Km) be identified and used to represent the affinity between the enzyme and the substrate?arrow_forward
- (a) Describe in detail how you will determine the primary structure of protein. You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows: Histidine 7.64 Lysine 9.74 Cystenie 5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.arrow_forwardNet charge and isoelectric point of an amino acid with an ionizable side group.Consider the net charge and isoelectric point of an amino acid with ionizable side (R-) group.(a) Identify the acidic amino acid(s) capable of having a negatively charged carboxyl side group.(b) Identify the basic amino acid(s) capable of having a positively charged amino side group.(c) For an amino acid with a side (R-) chain that can ionize to a negative charge, derive a general expression in terms of measured pH and known pKa values of α-carboxyla-amino (pKca), α-amino(pKaa),and side group (pKRa), respectively, for the net charge of an amino acid Consider the net charge and isoelectric point of an amino acid with ionizable side (R-) group.(d) For an amino acid with a side (R-) chain that can ionize to a positive charge, derive a general expression in terms of measured pH and known pKa values ofα-carboxyl (pKca), α-amino (pKaa), and side group (pKRa), respectively, for the net charge of the amino acid.(e)…arrow_forwardChemistry Estimate the pI of a dipeptide Cys-Asp assuming that the pKa values for αα-NH3+, αα-COOH, side chain of Cys and side chain of Asp are 8.0, 3.5, 8.5, and 3.9, respectively. Round your answer to one decimal place.arrow_forward
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