Organic Chemistry
8th Edition
ISBN: 9781305580350
Author: William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 27.4, Problem 27.6P
Deduce the amino acid sequence of an undecapeptide (11 amino acids) from the experimental results shown in the table.
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
ball & stick <
+ labels
This amino acid is
W
Give only typing answer with explanation and conclusion
Select the single best answer.
Watson and Crick determined that the DNA molecule has two helical strands. Each strand is made up
which consist of a base, a deoxyribose, and a phosphate group linked together.
of
What word most correctly fills in the blank in the preceding statement?
nucleotides
fatty acids
monosaccharides
amino acids
Chapter 27 Solutions
Organic Chemistry
Ch. 27.1 - Of the 20 protein-derived amino acids shown in...Ch. 27.2 - Prob. 27.2PCh. 27.2 - Prob. 27.3PCh. 27.3 - Draw a structural formula for Lys-Phe-Ala. Label...Ch. 27.4 - Which of these tripeptides are hydrolyzed by...Ch. 27.4 - Deduce the amino acid sequence of an undecapeptide...Ch. 27.6 - Prob. 27.7PCh. 27 - What amino acid does each abbreviation stand for?...Ch. 27 - The configuration of the chiral center in -amino...Ch. 27 - Assign an R or S configuration to the chiral...
Ch. 27 - Prob. 27.11PCh. 27 - Prob. 27.12PCh. 27 - Draw zwitterion forms of these amino acids. (a)...Ch. 27 - Prob. 27.14PCh. 27 - Why is Arg often referred to as a basic amino...Ch. 27 - Prob. 27.16PCh. 27 - Prob. 27.17PCh. 27 - Prob. 27.18PCh. 27 - Prob. 27.19PCh. 27 - Prob. 27.20PCh. 27 - Both norepinephrine and epinephrine are...Ch. 27 - Prob. 27.22PCh. 27 - Draw a structural formula for the form of each...Ch. 27 - Prob. 27.24PCh. 27 - Write the zwitterion form of alanine and show its...Ch. 27 - Prob. 27.26PCh. 27 - Write the form of aspartic acid most prevalent at...Ch. 27 - Prob. 27.28PCh. 27 - Prob. 27.29PCh. 27 - For lysine and arginine, the isoelectric point,...Ch. 27 - Prob. 27.31PCh. 27 - Account for the fact that the isoelectric point of...Ch. 27 - Prob. 27.33PCh. 27 - Prob. 27.34PCh. 27 - At pH 7.4, the pH of blood plasma, do the majority...Ch. 27 - Prob. 27.36PCh. 27 - Prob. 27.37PCh. 27 - Prob. 27.38PCh. 27 - A chemically modified guanidino group is present...Ch. 27 - Draw a structural formula for the product formed...Ch. 27 - Prob. 27.41PCh. 27 - Prob. 27.42PCh. 27 - A decapeptide has the following amino acid...Ch. 27 - Following is the primary structure of glucagon, a...Ch. 27 - Prob. 27.45PCh. 27 - Draw a structural formula of these tripeptides....Ch. 27 - Estimate the pI of each tripeptide in Problem...Ch. 27 - Glutathione (G-SH), one of the most common...Ch. 27 - Following are a structural formula and a...Ch. 27 - Prob. 27.50PCh. 27 - Prob. 27.51PCh. 27 - Prob. 27.52PCh. 27 - Prob. 27.53PCh. 27 - Prob. 27.54PCh. 27 - Distinguish between intermolecular and...Ch. 27 - Prob. 27.56PCh. 27 - Prob. 27.57P
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
- 22-84 How many different dipeptides can be made (a) using only alanine, tryptophan, glutamic acid, and arginine and (b) using all 20 amino acids?arrow_forward22-49 Based on your knowledge of the chemical properties of amino acid side chains, suggest a substitution for leucine in the primary structure of a protein that would probably not change the character of the protein very much.arrow_forwardDraw a segment of the backbone of a protein that is long enough for three peptide linkages to be present.arrow_forward
- Consider the tripeptide tyrosylleucylisoleucine. a. Specify its structure using three-letter symbols for the amino acids. b. How many peptide bonds are present within the peptide? c. Which of the amino acid residues has the largest R group? d. Which of the amino acid residues, if any, has an acidic side chain?arrow_forwardConsider the tripeptide leucylvalyltryptophan. a. Specify its structure using three-letter symbols for the amino acids. b. How many peptide bonds are present within the peptide? c. Which of the amino acid residues has the largest R group? d. Which of the amino acid residues, if any, has a basic side chain?arrow_forwardComplete hydrolysis of a 100.00-g sample of a peptide gave the following amounts of individual amino acids (molarmasses, in g/mol, appear in parentheses):3.00 g of glycine (75.07) ;0.90 g of alanine (89.10);3.70 g of valine (117.15);6.90 g of proline (115.13);7.30 g of serine (105.10);86.00 g of arginine (174.21);(a) Why does the total mass of amino acids exceed the mass of peptide? (b) What are the relative numbers of amino acids in the peptide? (c) What is the minimum molar mass of the peptide?arrow_forward
- A solution contains serine and alanine. What are the possible dipeptide products that can form from this mixture? H H H H N C -H N C O-H H CH₂OH H CH3 serine (ser) alanine (ala) Enter each answer as two three-letter codes joined with a dash (e.g. ala-ala).arrow_forwardConsider the amino acid glycine. Note: Reference the Naturally-occurring amino acids table for additional information. Draw the neutral form of the amino acidarrow_forwardAs we’ve discussed, a peptide bond is made when amino group of one amino acid combines with the carboxylic acid group of another amino acid (releasing a water molecule in the process). The C-N bond formed in this process is called a peptide bond. Peptide bonds have a few properties that might be unexpected. b) Another observation is that although the N-H of the peptide bond is able to serve as a H-bond donor the N atom of the peptide bond does not serve as an effective H-bond acceptor. Provide an explanation for this observation, using Lewis structures, VSEPR theory and/or valence bond theory as appropriate.c) It is also fairly accepted that while proteins undergo dynamic motions and conformational changes, and while R groups can freely rotate about Cα, it is generally not possible to freely rotate around a peptide bond. Please explain this observation, using a picture showing relevant orbitals on relevant atoms (your answer for part (a) might provide a useful basis for your reasoning…arrow_forward
- Use the following pentapeptide (5 amino acids linked together) structure and draw it again with the following amino acid sequence: glutamine, glycine, serine, alanine threonine. (Hint: You will have to look up the atoms that make up the R groups of the amino acids to replace the generic "R" in the structural formula provided). HH OHH OHH OHH OH HO | | || | | || | |||| | || | | || H-N-C-C-N-C-C-N-C-C-N-C-C-N-C-C-OH R R R R I Rarrow_forwardShown are the configuration of a gel electrophoresis experiment. Charged plates establish an electric field on a region of gel between the plates. A solution of DNA fragments, which acquire a negative charge in solution, is analyzed by using an electric field to drive the fragments through the gel. A drag force opposes the motion, causing the fragments to move at a constant speed. Larger fragments move more slowly, so the fragments separate by size to give a “fingerprint” of the sample. What is the energy transformation as the fragments move through the gel?A. Electric potential energy to kinetic energyB. Electric potential energy to thermal energyC. Electric potential energy to kinetic energy and thermal energyD. Kinetic energy to thermal energyarrow_forwardShow a dipeptide with two of your amino acids bonded to each other. Draw the structure. The amino acid is TRYPTOPHANarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
World of ChemistryChemistryISBN:9780618562763Author:Steven S. ZumdahlPublisher:Houghton Mifflin College Div
Introduction to General, Organic and BiochemistryChemistryISBN:9781285869759Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar TorresPublisher:Cengage Learning
Chemistry: Matter and ChangeChemistryISBN:9780078746376Author:Dinah Zike, Laurel Dingrando, Nicholas Hainen, Cheryl WistromPublisher:Glencoe/McGraw-Hill School Pub Co
Introductory Chemistry: An Active Learning Approa...ChemistryISBN:9781305079250Author:Mark S. Cracolice, Ed PetersPublisher:Cengage Learning
General, Organic, and Biological ChemistryChemistryISBN:9781285853918Author:H. Stephen StokerPublisher:Cengage Learning
Organic And Biological ChemistryChemistryISBN:9781305081079Author:STOKER, H. Stephen (howard Stephen)Publisher:Cengage Learning,
World of Chemistry
Chemistry
ISBN:9780618562763
Author:Steven S. Zumdahl
Publisher:Houghton Mifflin College Div
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
Chemistry: Matter and Change
Chemistry
ISBN:9780078746376
Author:Dinah Zike, Laurel Dingrando, Nicholas Hainen, Cheryl Wistrom
Publisher:Glencoe/McGraw-Hill School Pub Co
Introductory Chemistry: An Active Learning Approa...
Chemistry
ISBN:9781305079250
Author:Mark S. Cracolice, Ed Peters
Publisher:Cengage Learning
General, Organic, and Biological Chemistry
Chemistry
ISBN:9781285853918
Author:H. Stephen Stoker
Publisher:Cengage Learning
Organic And Biological Chemistry
Chemistry
ISBN:9781305081079
Author:STOKER, H. Stephen (howard Stephen)
Publisher:Cengage Learning,
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY