Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN: 9781305389892
Author: Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 3, Problem 8TYK
The first and major effect in denaturation of proteins is that:
a. peptide bonds break.
b. α helices unwind.
c. β sheet structures unfold.
d. tertiary structure is changed.
e. quaternary structures disassemble.
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
Which of the following is NOT an example of protein secondary structure?
a. alpha-helix
b. beta sheets
c. beta turn
d. coiled coil
e. loops
Which of the following statements are correct about the native state of a protein (select all that apply)?
A.
Polar sidechains commonly interact with water
B.
Hydrophobic amino acids tend to be on surface of protein
C.
The sidechains of polar amino acids are most commonly found in the central core of a protein
D.
Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains.
E.
Secondary structure is largely driven by hydrophobic interactions
Which of the following statements are correct about protein structure (select all that apply)?
A.
Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein
B.
Only amino acids with a net charge may interact with other amino acids
C.
The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role.
D.
Hydrophobic interactions play a key role in protein folding
E.
Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acids
Chapter 3 Solutions
Biology: The Dynamic Science (MindTap Course List)
Ch. 3.1 - What is the difference between hydrocarbons and...Ch. 3.1 - What is the maximum number of bonds that a carbon...Ch. 3.1 - Do carboxyl groups, amino groups, and phosphate...Ch. 3.1 - What is the difference between a dehydration...Ch. 3.2 - What is the difference between a monosaccharide, a...Ch. 3.3 - What are the three most common lipids in living...Ch. 3.4 - Prob. 1SBCh. 3.4 - What is a peptide bond, and what type of reaction...Ch. 3.4 - Prob. 3SBCh. 3.5 - What is the monomer of a nucleic acid...
Ch. 3.5 - What are the chemical differences between DNA and...Ch. 3 - Which functional group has a double bond and forms...Ch. 3 - Which of the following characteristics is not...Ch. 3 - Cellulose is to carbohydrate as: a. amino acid is...Ch. 3 - Maltose, sucrose, and lactose differ from one...Ch. 3 - Lipids that are liquid at room temperature: a. are...Ch. 3 - Which of the following statements about steroids...Ch. 3 - The term secondary structure refers to a proteins:...Ch. 3 - The first and major effect in denaturation of...Ch. 3 - In living systems: a. proteins rarely combine with...Ch. 3 - RNA differs from DNA because: a. RNA may contain...Ch. 3 - Discuss Concepts Identify the following structures...Ch. 3 - Discuss Concepts Lipoproteins are relatively...Ch. 3 - Prob. 13TYKCh. 3 - Prob. 14TYKCh. 3 - Prob. 15TYKCh. 3 - Prob. 1ITDCh. 3 - Prob. 2ITDCh. 3 - Prob. 3ITD
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
- Proteins are the dominant structural and functional molecules in a cell. Which one of the following statements about proteins is NOT correct? A. The native conformation of a protein is usually arrived at very quickly after synthesis. B. Hydrogen bonding is the only type of bonding that gives rise to secondary structure. C. Urea denatures proteins by disrupting the interactions among non-polar (hydrophobic) amino acids D. Most proteins consist of a single polypeptide and thus do not have quaternary structure.arrow_forwardWhich of the following is NOT TRUE about secondary structure in proteins? (More than one may apply) A. Stabilized by non-covalent bonds B. Is illustrated by DnaA molecules interacting in the ori C. Unravels at high temperatures when intramolecular non-covalent bonds are destroyed D. Occurs in a subregion of a protein E. Exemplified by beta sheets F. Describes the order of amino acids in a polypeptidearrow_forwardThe level of protein structure that describes all aspects of the three-dimensional folding of a polypeptide is referred to as the A. quaternary structure. B. secondary structure. C. primary structure. D. tertiary structure.arrow_forward
- Match the level of protein structure to its description: Primary Secondary Tertiary Quaternary A. Folding due to interactions among the peptide backbone B. Interactions among multiple polypeptide chains C. Sequence of amino acids D. Folding due to interactions among side chainsarrow_forwardWhich of the following statements is/are TRUE for globular proteins? A. sensitive to changes in pH & heat B. regular amino acid sequence C. soluble in water D. structural rolearrow_forwardWhich of the following statement about quaternary structure of protein is correct? Select one: a. Quaternary structure is a force between different polypeptides. b. Hydrogen bond is an only force found in quaternary structure. c. Quaternary structure contains one polypeptide. d. Quaternary structure is an unfolded form of protein.arrow_forward
- Which of the following is an example of protein denaturation? * A. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone. B. Several amino acids are joined together together via peptide bonds. C. A protein binds with with a substrate, lowering the activation energy of reaction. D. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be left with only its primary structure. E. Results to unfolding, partial or incomplete disorganization of the protein's secondary and tertiary structure.arrow_forwardIn extracellular proteins the amino acid Cys can interact with another Cys to form a __bond sometimes called ________. The formation of this covalent bond is a reaction. a. O b. disulfide, cystine, oxidizing c. disulfide, cysteine, reducing d. disulfide, cystine, dehydration O e. peptide, polypeptide, oxidizing peptide, polypeptide, condensationarrow_forwardWhich of the following events would have the strongest influence on the overall three-dimensional structure of a protein? Select one: a. Valines angle away from surrounding water molecules as the protein folds b. Two polypeptide strands, running in opposite directions, form hydrogen bonds with each other Oc. Another protein sticks to its outside d. The amine and carboxylic ends of the protein chain are left unreacted Oe. Three glycines are chained together Clear my choice Previous page esc ! 1 ← 2 3 W 3 E 38 $ 4 R 5 T 80 MacBook Pro A 6 Y & 7 U 8 I 9 4 1 O 0 P TO + ( W Next paarrow_forward
- This structure of a protein comes from the further bending and folding of pleated sheets and helices: A. primary B. secondary C. tertiary D. quaternaryarrow_forwardDenaturation of a protein A. adds hydrogen bonds to the primary level of protein structure. B. breaks hydrogen bonds in the primary level of protein structure. C. adds hydrogen bonds to the secondary and tertiary levels of protein structure. D. breaks hydrogen bonds in the secondary and tertiary levels of protein structure.arrow_forwardWhich of the following statement about proteins is correct a. alpha helix and Beta pleated sheets are considered quaternary structures b. a single polypeptide only has primary sytructure, secondary, tertiary, and quaternary structures require more than one polypeptide c. there are 30 essential amino acids that are the monomer building blocks of proteins d. polypeptides have a distinct polarity (directionality) with one end refered to as the free amino end, and the other called the free carboxyl endarrow_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:PEARSON
Biology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax
Anatomy & 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 & Company
Laboratory 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