Organic Chemistry (8th Edition)
8th Edition
ISBN: 9780134042282
Author: Paula Yurkanis Bruice
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 21.4, Problem 12P
Interpretation Introduction
Interpretation:
The
Concept introduction:
The isoelectric point (
The value of
If the amino acid has ionizable side chain, then the
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
8. The following proteins represent a wide range of molecular weights and
isoelectric points. Mr is the molecular weight of a single protein chain.
• Protein 1: Mr 68,544; pl 6.11 (monomer)
• Protein 2: Mr 29,041; pl 5.32 (dimer)
• Protein 3: Mr 15,805; pl 5.7 (dimer)
• Protein 4: Mr 12,165; pl 4.74
a. Which protein is the most acidic? Explain your answer.
b. Which protein will migrate the slowest in an SDS-PAGE? Explain your
answer.
c. In what order will these proteins elute from a cation exchanger at pH 8?
Explain your answer.
d. In what order will these proteins salt out from a pH 7 solution by the
dropwise addition of saturated ammonium sulfate? Explain your answer.
5
83°F Cloudy
Among these protein assays, which work in acidic conditions?
a. Biuret assay
b. Bicinchoninic acid assay
c. Bradford assay
d. Lowry assay
Would serine or cysteine be the better antidote against heavy metals? Briefly rationalize your answer.
Chapter 21 Solutions
Organic Chemistry (8th Edition)
Ch. 21.1 - a. Explain why, when the imidazole ring of...Ch. 21.2 - a. Which isomer(R)-alanine or (S)-alanineis...Ch. 21.2 - Prob. 4PCh. 21.3 - Prob. 5PCh. 21.3 - Prob. 6PCh. 21.3 - Draw the predominant form for glutamate in a...Ch. 21.3 - a. Why is the pKa of the glutamate side chain...Ch. 21.4 - Calculate the pI of each of the following amino...Ch. 21.4 - a. Which amino acid has the lowest pI value? b....Ch. 21.4 - Prob. 12P
Ch. 21.4 - Prob. 13PCh. 21.4 - Explain why the pI of lysine is the average of the...Ch. 21.5 - What aldehyde is formed when valine is treated...Ch. 21.5 - Prob. 16PCh. 21.5 - Prob. 17PCh. 21.5 - Prob. 18PCh. 21.5 - Prob. 19PCh. 21.6 - Why is excess ammonia used in the preceding...Ch. 21.6 - Prob. 21PCh. 21.6 - What amino acid is formed using the...Ch. 21.6 - Prob. 23PCh. 21.6 - What amino acid is formed when the aldehyde used...Ch. 21.7 - Esterase is an enzyme that catalyzes the...Ch. 21.8 - Draw the tetrapeptide Ala-Thr-Asp-Asn and indicate...Ch. 21.8 - Draw the resonance contributors of the peptide...Ch. 21.8 - Which bonds in the backbone of a peptide can...Ch. 21.9 - An opioid pentapeptide has the following...Ch. 21.9 - What is the configuration about each of the...Ch. 21.9 - Glutathione is a tripeptide whose function is to...Ch. 21.10 - What dipeptides would be formed by heating a...Ch. 21.10 - Suppose you are trying to synthesize the dipeptide...Ch. 21.10 - Show the steps in the synthesis of the...Ch. 21.10 - a. Calculate the overall yield of bradykinin when...Ch. 21.11 - Show the steps in the synthesis of the...Ch. 21.13 - Prob. 37PCh. 21.13 - In determining the primary structure of insulin,...Ch. 21.13 - A decapeptide undergoes partial hydrolysis to give...Ch. 21.13 - Explain why cyanogen bromide does not cleave on...Ch. 21.13 - Indicate the peptides produced from cleavage by...Ch. 21.14 - Prob. 43PCh. 21.14 - Three peptides were obtained from a trypsin...Ch. 21.14 - Prob. 45PCh. 21.15 - How would a protein that resides in the nonpolar...Ch. 21.16 - a. Which would have the greatest percentage of...Ch. 21.17 - When apples that have been cut are exposed to...Ch. 21 - Glycine has pK2 values of 2.34 and 9.60. At what...Ch. 21 - Prob. 50PCh. 21 - A titration curve is a plot of the pH of a...Ch. 21 - Prob. 52PCh. 21 - Aspartame (its structure is on page 1007) has a pl...Ch. 21 - Draw the form of aspartate that predominates at...Ch. 21 - Show how phenylalanine can be prepared by...Ch. 21 - A professor was preparing a manuscript for...Ch. 21 - What aldehydes are formed when the following amino...Ch. 21 - Prob. 58PCh. 21 - Determine the amino acid sequence of a polypeptide...Ch. 21 - Prob. 60PCh. 21 - Prob. 61PCh. 21 - Which is the more effective buffer at...Ch. 21 - Identify the location and type of charge on the...Ch. 21 - Draw the product obtained when a lysine side chain...Ch. 21 - After the polypeptide shown below was treated with...Ch. 21 - Treatment of a polypeptide with 2-mercaptoethanol...Ch. 21 - Show how aspartame can be synthesized using DCCD.Ch. 21 - -Amino acids can be prepared by treating an...Ch. 21 - Reaction of a polypeptide with carboxypeptidase A...Ch. 21 - a. How many different octapeptides can be made...Ch. 21 - Glycine has pKa values of 2.3 and 9.6. Do you...Ch. 21 - A mixture of 15 amino acids gave the fingerprint...Ch. 21 - Write the mechanism for the reaction of an amino...Ch. 21 - Prob. 74PCh. 21 - Show how valine can be prepared by a. a...Ch. 21 - The primary structure of -endorphin, a peptide...Ch. 21 - A chemist wanted to test his hypothesis that the...Ch. 21 - Propose a mechanism for the rearrangement of the...Ch. 21 - A normal polypeptide and a mutant of the...Ch. 21 - Determine the amino acid sequence of a polypeptide...
Knowledge Booster
Learn more about
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
- Explain why a protein is least soluble in an aqueous medium that has a pH equal to the isoelectric point of the protein.arrow_forwardA 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)arrow_forwardWhat special role does the amino acid cysteine have in the peptides vasopressin and oxytocin?arrow_forward
- Draw structures from notations or notations from structures, for the following tripeptides. (EOCQ 62) it. For drawing the structure of a tripeptide, follow the hints given in the previous question; you will have to connect three amino acid molecules in the specified order. а. Cys-Gly-Ala b. Ser-Leu-Val Нон НОН Но С. H,N-C-C-N-Ç-C-N-C-C-OH CH,CH,CHCH, CH3 C,H,CH, НОНН онНО d. H,N-C-C-N-C-C-N-Ç-C-OH CH,SCH,CH, CH-CНОН НSCH,arrow_forwardPlease solve thisarrow_forwardAlthough 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_forward
- What amino acid substitution would be accompanied by the largest decrease in enteric water penalty? a. Substitution of Arg with Tyr on an exposed surface of a protein. 6. Replacing lle with Asp on an unexposed surface of a protein. c. Replacing Leu with Thr on an exposed surface of a protein. d. None of the above would increase water entropy.arrow_forwardDetermine the type of stereoisomer the following amino acid is. HI!!! 000 A. This is a D-amino acid. This is also a R-atnino acid. B. This is a L-amino acid. This is also a R- anuno acid. C. This is a D- amino acid. This is also a S-amino acid. x D. This is a L-amino acid. This is also a S-amino acid.arrow_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
- 4: Draw structures from notations or notations from structures, for the following dipeptides. Look up in book for the structures of various amino acids and their names (and notations). (EOCQ 60) Hints for drawing a dipeptide from the specified amino acids. From the given symbols (Ser, Thr, etc), draw the structures for the amino acids in the specified order example, for Ser-Thr, draw Serine first and then Threonine). Then remove the OH from the first amin and one H (from the N atom) on the second amino acid. Then join the remaining fragments; that give the dipeptide formed. In these reactions, H2O is formed as a side product; but it is implied, and you have to show it in your answers. The following equation illustrates that. Here, R and R' are symbolic. In an actual question, you must the actual structures for the amino acids (Table 16.3 in the book). O H || | Н.N— CH— С-N-CH—С-ОН H,N-CH-C–OH + H,N-CH-Ċ–OH R' R. R' (H2O is a sid no need t Amino acid 2 dipeptide Amino acid 1 а. Cys-Ser…arrow_forward2. Describe the basic chemical requirements for the aminoglycosides. Why are these compounds strongly basic and exist as polycations at physiological pH? (Use equations to explain). OH OH HỌ H2N HO FHO- Но Но NH2 H,N NH2arrow_forwardWhich R group would most likely be found in a hydrophobic area of the tertiary structure of a globular protein? * A. -CH3 В. -СH,ОН C. -CH,COO- D. -SH Е. -СH, CONH,arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Chemistry & Chemical ReactivityChemistryISBN:9781337399074Author:John C. Kotz, Paul M. Treichel, John Townsend, David TreichelPublisher:Cengage LearningChemistry & Chemical ReactivityChemistryISBN:9781133949640Author:John C. Kotz, Paul M. Treichel, John Townsend, David TreichelPublisher:Cengage LearningChemistry: Principles and ReactionsChemistryISBN:9781305079373Author:William L. Masterton, Cecile N. HurleyPublisher:Cengage Learning
- Chemistry for Today: General, Organic, and Bioche...ChemistryISBN:9781305960060Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. HansenPublisher:Cengage LearningIntroductory Chemistry: An Active Learning Approa...ChemistryISBN:9781305079250Author:Mark S. Cracolice, Ed PetersPublisher:Cengage LearningIntroduction to General, Organic and BiochemistryChemistryISBN:9781285869759Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar TorresPublisher:Cengage Learning
Chemistry & Chemical Reactivity
Chemistry
ISBN:9781337399074
Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Publisher:Cengage Learning
Chemistry & Chemical Reactivity
Chemistry
ISBN:9781133949640
Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Publisher:Cengage Learning
Chemistry: Principles and Reactions
Chemistry
ISBN:9781305079373
Author:William L. Masterton, Cecile N. Hurley
Publisher:Cengage Learning
Chemistry for Today: General, Organic, and Bioche...
Chemistry
ISBN:9781305960060
Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Publisher:Cengage Learning
Introductory Chemistry: An Active Learning Approa...
Chemistry
ISBN:9781305079250
Author:Mark S. Cracolice, Ed Peters
Publisher:Cengage Learning
Introduction to General, Organic and Biochemistry
Chemistry
ISBN:9781285869759
Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher:Cengage Learning