Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
8th Edition
ISBN: 9780134015187
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 18, Problem 18.88AP
Interpretation Introduction
Interpretation:
Minimum number of polypeptide chains necessary for quaternary structure of protein to exist is to be identified.
Concept introduction:
Peptide bond is an amide bond,
Any number of amino acid can link together to form a linear chain like
Quaternary structure of protein is forms when two or more proteins chains assemble when a larger three-dimensional structure held together by noncovalent interaction.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
What is the approximate molecular weight of a protein with 682 amino acid residues in a single polypeptide chain?
How many different tripeptides can be formed from three different amino acids, glutamine, histidine, and lysine? Draw the possible structures. Using three-letter abbreviations, give the names for all of the possible tripeptides.
Consider the structure of the tripeptide (in its fully protonated form) below.
H
H
H
+ I ||
H₂N-C-C-N-C-C-N-C-C-OH
1
I |
H CH₂ H CH₂
CH₂
T
C=O
OH
AA1
0=0
||
HC-CH3
CH3
AA2
AA3
0=C
1. Give the sequence of the tripeptide using the ONE-LETTER DESIGNATION (UPPERCASE LETTER) with NO spaces and symbols between each letter.
2. How many ionizable groups are there in the tripeptide? Give the numerical value (e.g., 10 not ten).
• pH 10: {Choices: -2, -1, 0, +1, +2}
3. Which amino acid residue has one ionizable group left upon forming the tripeptide? {Choices: AA1, AA2, AA3, none, all}
4. Give the net charge of the dominant structure of the tripeptide at the given pH values. The pK, values of the amino acids are given in Table 1.
• pH 4: {Choices: -2, -1, 0, +1, +2}
Chapter 18 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
Ch. 18.2 - Prob. 18.1PCh. 18.2 - Prob. 18.2PCh. 18.3 - Prob. 18.3PCh. 18.3 - Examine the ball-and-stick model of valine in the...Ch. 18.3 - Indicate whether each of the following molecules...Ch. 18.3 - Prob. 18.6PCh. 18.3 - Prob. 18.7KCPCh. 18.3 - Prob. 18.8PCh. 18.3 - Prob. 18.9PCh. 18.3 - Prob. 18.10P
Ch. 18.3 - Prob. 18.11PCh. 18.3 - Prob. 18.12PCh. 18.4 - The proteins collagen, bovine insulin, and human...Ch. 18.4 - Prob. 18.2CIAPCh. 18.4 - Prob. 18.13PCh. 18.4 - Prob. 18.14PCh. 18.5 - Valine is an amino acid with a nonpolar side...Ch. 18.5 - Tripeptides are composed of three amino acids...Ch. 18.5 - Prob. 18.17PCh. 18.5 - Identify the amino acids in the following...Ch. 18.5 - Prob. 18.19PCh. 18.5 - Prob. 18.3CIAPCh. 18.5 - Prob. 18.4CIAPCh. 18.5 - Two of the most complete (balanced) proteins...Ch. 18.6 - Prob. 18.6CIAPCh. 18.6 - Prob. 18.7CIAPCh. 18.6 - (a)What atoms are present in a planar unit in a...Ch. 18.6 - Prob. 18.21PCh. 18.6 - Prob. 18.22PCh. 18.7 - Prob. 18.23PCh. 18.7 - Prob. 18.24PCh. 18.7 - Complete the following two sentences with either...Ch. 18.7 - Prob. 18.26KCPCh. 18.8 - Which of the following pairs of amino acids can...Ch. 18.8 - Look at Table 18.3 and identify the type of...Ch. 18.8 - In Figure 18.3, identify the amino acids that have...Ch. 18.8 - Prob. 18.30PCh. 18.9 - Prob. 18.31PCh. 18.10 - Another endoprotease is trypsin. Trypsin...Ch. 18.10 - Prob. 18.33PCh. 18.10 - Prob. 18.8CIAPCh. 18.10 - Prob. 18.9CIAPCh. 18 - Draw the structure of the following amino acids,...Ch. 18 - Prob. 18.35UKCCh. 18 - Prob. 18.36UKCCh. 18 - Prob. 18.37UKCCh. 18 - Prob. 18.38UKCCh. 18 - Threonine has two chiral centers. Draw L-threonine...Ch. 18 - Name four biological functions of proteins in the...Ch. 18 - Prob. 18.41APCh. 18 - Prob. 18.42APCh. 18 - Prob. 18.43APCh. 18 - Prob. 18.44APCh. 18 - Prob. 18.45APCh. 18 - Prob. 18.46APCh. 18 - Prob. 18.47APCh. 18 - Draw leucine and identify any chiral carbon atoms...Ch. 18 - Prob. 18.49APCh. 18 - Prob. 18.50APCh. 18 - Is histidine hydrophilic or hydrophobic? Explain...Ch. 18 - Prob. 18.52APCh. 18 - At neutral pH, which of the following amino acids...Ch. 18 - Prob. 18.54APCh. 18 - Prob. 18.55APCh. 18 - Prob. 18.56APCh. 18 - Prob. 18.57APCh. 18 - Proteins are usually least soluble in water at...Ch. 18 - Prob. 18.59APCh. 18 - Prob. 18.60APCh. 18 - Prob. 18.61APCh. 18 - Prob. 18.62APCh. 18 - Prob. 18.63APCh. 18 - (a)Identify the amino acids present in the peptide...Ch. 18 - Prob. 18.65APCh. 18 - Prob. 18.66APCh. 18 - Prob. 18.67APCh. 18 - Prob. 18.68APCh. 18 - Prob. 18.69APCh. 18 - Prob. 18.70APCh. 18 - Prob. 18.71APCh. 18 - Prob. 18.72APCh. 18 - Prob. 18.73APCh. 18 - Prob. 18.74APCh. 18 - Prob. 18.75APCh. 18 - What kind of bond would you expect between chains...Ch. 18 - Is the bond formed between each pair in Problem...Ch. 18 - Prob. 18.78APCh. 18 - Prob. 18.79APCh. 18 - Prob. 18.80APCh. 18 - Prob. 18.81APCh. 18 - Prob. 18.82APCh. 18 - Prob. 18.83APCh. 18 - Prob. 18.84APCh. 18 - Prob. 18.85APCh. 18 - Prob. 18.86APCh. 18 - Prob. 18.87APCh. 18 - Prob. 18.88APCh. 18 - Give an example of a protein that has quaternary...Ch. 18 - Prob. 18.90APCh. 18 - Prob. 18.91APCh. 18 - Prob. 18.92APCh. 18 - Prob. 18.93APCh. 18 - Prob. 18.94APCh. 18 - Prob. 18.95APCh. 18 - Prob. 18.96APCh. 18 - Prob. 18.97APCh. 18 - Prob. 18.98CPCh. 18 - Prob. 18.99CPCh. 18 - Prob. 18.100CPCh. 18 - Prob. 18.101CPCh. 18 - Prob. 18.102CPCh. 18 - Prob. 18.103CPCh. 18 - Prob. 18.104CPCh. 18 - Prob. 18.105CPCh. 18 - Prob. 18.106CPCh. 18 - Prob. 18.107CPCh. 18 - Prob. 18.108CPCh. 18 - Prob. 18.109GPCh. 18 - Prob. 18.110GPCh. 18 - Prob. 18.111GPCh. 18 - Prob. 18.112GP
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Identify the following statements as descriptive of the secondary, tertiary, or quaternary structure of a protein. What types of interactions stabilize each type of structure?(a) The polypeptide chain has a number of bends and twists, resulting in a compact structure.(b) The polypeptide backbone forms a right-handed coil.(c) The four polypeptide chains are arranged in a spherical shape.arrow_forwardHow many reducing ends and non-reducing ends will a oligosaccharide have with 4 exact branch points in its structure?arrow_forwardDraw the structure of each of the following tripeptides:(a) Lysine-phenylalanine-threonine(b) Alanine-leucine-valine with the charges that exist in cell fluidarrow_forward
- Each amino acid in a run of several amino acid residues of a polypeptide chain have phi values of approximately -140° and psi values of +147°. What kind of structure is this likely to be?arrow_forwardif glutamic acid were replaced by proline in a protein, how would the tertiary structure be affected?arrow_forwardWithin a naturally-occurring polypeptide, under neutral pH conditions (pH = 7.0), which of the following amino acids always has a positively charged amine group? the first amino acid in the primary structure histidine lysine arginine the last amino acid in the primary structurearrow_forward
- Poly- L -leucine in an organic solvent such as dioxane is α helical, whereas poly- L -isoleucine is not. Why do these amino acids with the same number and kinds of atoms have different helix-forming tendencies?arrow_forwardConsider the following tetrapeptide, written in a sequence according to normal convention, from left to right: Residue 1 is acidic; Residue 2 is cysteine (an amino acid containing a CH2SH R-group); Residue 3 is proline (a large hydrophobic amino acid); Residue 4 is basic. Which of the following four general statements is TRUE regarding this tetrapeptide? Residue 2 belongs to the amino acid category known as "basic." 3 of these 4 responses are correct O This tetrapeptide does not have the ability to form a disulfide linkage with an identical tetrapeptide. The acidic residue (Residue #1) is at the amino terminus of this tetrapeptide. This tetrapeptide could be part of an alpha-helix, since the large size of the proline would not have any impact on the consistency of the spiral shape.arrow_forwardGiven that an α helix has 3.6 residues per turn and the rise along the α helix axis is 5.4 Å, approximately how many amino acids would you find in a single contiguous α helix that is 210 Å long?arrow_forward
- Why do think nucleotides are also sometimes referred to as “bases” or “nucleotide bases”? What is the difference between a nucleotide and a nucleoside? Explain by giving an example, using structures. What kind of bond links a base to some sugar? Is the sugar an alpha or beta anomer? In what position(s) of the sugar does this occur? In what position(s) of the base does this occur? Instead of the term “Formation of a nucleoside”, what could the name of the reaction be? What functional group is being formed? Define the primary structure of DNA/RNA. Compare and contrast to the primary structure of proteins.arrow_forwardWhat parts of a polypeptide participate in the bonds that hold together secondary and tertiary structure? Explain with the help of diagram.arrow_forwardConsider the following tetrapeptide, written in a sequence according to normal convention, from left to right: Residue 1 is acidic; Residue 2 is proline (a large hydrophobic amino acid); Residue 3 is cysteine (an amino acid containing a -CH2SH R-group); Residue 4 is basic. Which of the following four general statements is TRUE regarding this tetrapeptide? This tetrapeptide probably is not part of an alpha-helix, since the large size of the proline would disrupt the consistency of the spiral shape. Residue 3 belongs to the amino acid category known as "basic." This tetrapeptide has the ability to form a disulfide linkage with an identical tetrapeptide. The acidic residue (Residue #1) is at the amino terminus of this tetrapeptide. 3 of these 4 responses are correctarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
Macromolecules | Classes and Functions; Author: 2 Minute Classroom;https://www.youtube.com/watch?v=V5hhrDFo8Vk;License: Standard youtube license