WHAT IS LIFE? A GUIDE TO BIO 3E+LAUNCHPA
3rd Edition
ISBN: 9781319103316
Author: PHELAN
Publisher: Macmillan Higher Education
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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.
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Check out a sample textbook solutionStudents have asked these similar questions
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.
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
pentachloride
Which 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 quaternary
Chapter 2 Solutions
WHAT IS LIFE? A GUIDE TO BIO 3E+LAUNCHPA
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
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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
- 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
- 1. 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_forwardWhat maintains the secondary structure of protein: A) peptide bond. B) Hydrogen bonds between the amino group of one peptide bond and the carboxyl group of another peptide bond. C) Hydrogen bonds between the R group of one amino acid and the carboxyl group og another peptide bond. D) disulfide bonds. E) Hydrophobic interactions.arrow_forward
- Proper folding is essential for most proteins to function. Which of the following statement about protein folding are correct. There may be more than 1 right answer. a) changing the primary sequence will change the final conformation b) desaturation results in a protein that has a higher free energy than the native conformation c) protein spontaneously fold into their correct shape d) denatrutation will cause a protein to lose its tertiary structurearrow_forwarda) Can a carbon with a double bond have a D or L designation? Explain. b) name and describe the levels of protein structure. c)What is the complementary bass player for the following sequence: CGATAATGC. d) in base pairing, why do we never see AG, GA, CT or TC forming complementary base pairs? e) why is vegetarianism a more energy intensive process (from the organism standpoint) than being omnivores? [DON'T EVEN THINK OF STATING ANYTHING ABOUT FIBER, BULK, AND/OR CELULOSE!!!!] f) why is significant serum (in the bloodstream) cholesterol reduction so difficult, and why do most of the drugs designed to reduce cholesterol target the liver?arrow_forwardWhich of the following is not known to be involved in the process of assisted folding of proteins? OA) Chaperonins OB) Disulfide interchange OC) Heat shock proteins OD) Peptide bond hydrolysis OE) Peptide bond isomerizationarrow_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY