Loose-leaf Version for What is Life? A Guide to Biology
3rd Edition
ISBN: 9781464172274
Author: Jay Phelan
Publisher: W.H. Freeman & Co
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 2, Problem 16MC
Summary Introduction
Introduction:
The quaternary structure of proteins is formed when different polypeptide strands come together in their folded forms to form a complete protein.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
2. Identify the structural level in each protein.
A) quaternary structure
B) tertiary structure
C) secondary structure
D) primary structure
1) The protein folds into a compact structure stabilized by interactions between R groups.
2) the combination of two or more protein molecules to form an active protein
3) B-pleated sheet
4) the peptide bonds betwecen the amino acids
5) the structural level achieved when hydrogen bonds form between the carboxyl group of one amino
acid and the amino group of a different amino acid
Water-soluble proteins such as myoglobin tend to fold such that:
A) hydrophobic amino acids R-groups are on the interior of the protein and
hydrophilic groups are on the outside
OB) all peptides form hydrogen bonds with water.
C) hydrophilic amino acid R-groups are on the interior of the protein and
hydrophobic groups are on the outside.
O D) hydrophilic and hydrophobic amino acid R-groups form hydrogen bonds with
each other.
The substitution of one amino acid for another in a polypeptide chain can affect the __________ of the resulting protein.
A) primary structure
B) secondary structure
C) tertiary structure
D) quaternary structure
E) all levels of protein structure can be affected by substituting one amino acid for another.
Chapter 2 Solutions
Loose-leaf Version for What is Life? A Guide to Biology
Ch. 2 - Prob. 1SACh. 2 - Prob. 2SACh. 2 - Prob. 3SACh. 2 - Prob. 4SACh. 2 - Prob. 5SACh. 2 - Prob. 6SACh. 2 - Prob. 7SACh. 2 - Prob. 8SACh. 2 - Prob. 9SACh. 2 - Prob. 10SA
Ch. 2 - Prob. 11SACh. 2 - Prob. 12SACh. 2 - Prob. 13SACh. 2 - Prob. 14SACh. 2 - Prob. 15SACh. 2 - Prob. 16SACh. 2 - Prob. 17SACh. 2 - Prob. 18SACh. 2 - Prob. 19SACh. 2 - Prob. 20SACh. 2 - Prob. 1MCCh. 2 - Prob. 2MCCh. 2 - Prob. 3MCCh. 2 - Prob. 4MCCh. 2 - Prob. 5MCCh. 2 - Prob. 6MCCh. 2 - Prob. 7MCCh. 2 - Prob. 8MCCh. 2 - Prob. 9MCCh. 2 - Prob. 10MCCh. 2 - Prob. 11MCCh. 2 - Prob. 12MCCh. 2 - Prob. 13MCCh. 2 - Prob. 14MCCh. 2 - Prob. 15MCCh. 2 - Prob. 16MCCh. 2 - Prob. 17MCCh. 2 - Prob. 18MCCh. 2 - Prob. 19MC
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- K. A protein which has more than one stable conformation is called a: a) chaperone protein b) molten globule c) flexible protein d) inherently unstructured protein L. If a denatured protein does not spontaneously renature upon removal of denaturing agents, it may require a_to renature. a) chaperone protein b) molten globule c) flexible protein d) inherently unstructured protein M. Prion protein and amyloid protein have which trait in common? A) They denature very easily b) they are both unstable forms of ribonuclease c) they bind strongly to hemoglobin d) they both may assume a fibrous form which is damaging to brain tissue N. Which of these statements about hemoglobin is NOT true? A) it is a tetrameric globular protein b) it has a prosthetic group called heme c) it's dominant motif is beta barrel d) its dominant motif is helix-turn-helix O. The reagent used to break disulfide bonds is: a) urea b) beta-mercaptoethanol c) guanidine hydrochloride d) phosphorus pentachloridearrow_forwardThe protein pictured has .. O A) primary structure B) secondary structure C) tertiary structure D) quaternary structure E) all of the abovearrow_forwardWhich of the following levels of protein structure can involve covalent bond formation? A) Primary B) Secondary C) Teritary D) Quaternary E) Primary and teritary F) Primary, teritary and quaternaryarrow_forward
- The tertiary structure of a protein is the : A) overall protein structure resulting from the aggregation of two or more polypeptide subunits. B) order in which amino acids are joined in a polypeptide chain. C) bonding together of several polypeptide chains by weak bonds. D)organization of a polypeptide chain into an α helix or β pleated sheet. E)unique three-dimensional shape of the fully folded polypeptide.arrow_forwardWhat is the CORRECT way to classify the protein below according to its secondary- structure elements? un a) not possible to determine b) all a ○ c) alẞ Od) a + B e) all Barrow_forwardWhich of the following statements is true about the quaternary structure of a protein? A) The quaternary structure of a protein is based on how polypeptide subunits interact with one another. B) The quaternary structure of a protein is affected by hydrogen bonds. C) The quaternary structure is the overall shape of a protein. D) The quaternary structure is driven by a- helices and B-pleated sheets. E) The quaternary structure is found in all proteins.arrow_forward
- 10) Denaturation of a protein A) changes the primary structure of a protein. B) disrupts the secondary, tertiary, or quaternary structure of a protein. C) is always irreversible. D) hydrolyzes peptide bonds.arrow_forwardFor each of the following amino acids: 1) describe what the important functional group of the amino acid side chain is, 2) identify the charge of the side chain, 3) name another component in the structure that the amino acid might interact with, and 4) indicate how the interaction with the component listed in 3) might be occurring (i.e., electrostatic interaction, hydrogen bond, hydrophobic interaction, etc.) a) Asp153 b) Arg166 c) Lys167arrow_forwardWhich level(s) of protein structure result(s) from non-covalent interactions involving both backbone groups and side chains? (Select all that apply!) a) Primary b) Secondary c) Tertiary d) Quaternaryarrow_forward
- A coiled peptide chain held in place by hydrogen bonding between peptide bonds in the same chain is : A) Alpha helix B) Primary structure C) Tertiary structure E) Beta pleated sheetsarrow_forward1. Which one of the following is NOT an important functional group or linkage in biomolecules? A) Phosphodiester B) Hemiketal C) Thiol D) Lipid E) Phosphoanhydridearrow_forwardWhich of the following features correctly describe aspects of protein structure? a) A protein possessing disulfide bonds will be more stable than a protein with the identical primary sequence lacking disulfide bonds. O b) B-sheets can only be formed from the anti-parallel arrangement of B-strands. c) Folding of a protein (tertiary structure) will typically result in a majority of the non-polar amino acids being distributed on the protein surface. d) both a and carrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSONBiology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStaxAnatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
- Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & CompanyLaboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:9780815344322
Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)
Biology
ISBN:9781260231700
Author:Sylvia S. Mader, Michael Windelspecht
Publisher:McGraw Hill Education
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY