Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 5, Problem 13TYK
What happens when a protein denatures?
- a. Its primary structure is disrupted.
- b. Its secondary and tertiary structures are disrupted.
- c. It flips inside out.
- d. Its hydrogen bonds, ionic bonds, hydrophobic interactions, disulfide bridges, and peptide bonds are disrupted.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Describe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)
Why do some proteins contain D-amino acids?
A. D-amino acids will determine the binding of the protein to its
interacting partners.
B. D-amino acids will determine whether the structure will be
recognized and digested by naturally occurring enzymes
C. D-amino acids determines the reactions the proteins will undergo.
D. D-amino acids determines the solubility of the protein in aqueous
solution.
OE. A combination of D and L-amino acids is necessary for the proper
folding of protein structures in aqueous solutions.
A protein in its native three dimensional conformation is cleaved with trypsin. According to the amino acid sequence, there are 9 residues where trypsin could cleave, yet only 3 fragments were produced from the digest. What conclusion can be made about protein structure that would lead to this result?
The protein has multiple domains
b.
The protein is highly compacted, minimally accessible by solvent molecules
c.
The protein has quaternary structure
d.
The protein has a dynamic structure, highly accessible by solvent molecules
e.
The protein is compromised only of alpha helices
Chapter 5 Solutions
Study Guide for Campbell Biology
Ch. 5 - Monomers are linked into polymers by ________...Ch. 5 - You can recognize a monosaccharide by its multiple...Ch. 5 - Number the carbons in the following glucose and...Ch. 5 - Prob. 4IQCh. 5 - Fill in this concept map to help you organize your...Ch. 5 - a. Draw the amino acids alanine (R group: CH3) and...Ch. 5 - In the following diagram of a portion of a...Ch. 5 - Now that you have gained experience with concept...Ch. 5 - a. Label the three parts of this nucleotide....Ch. 5 - Take the time to create a concept map that...
Ch. 5 - Prob. 1SYKCh. 5 - Prob. 2SYKCh. 5 - glycogen A. carbohydrate B. lipid C. protein D....Ch. 5 - cholesterol A. carbohydrate B. lipid C. protein D....Ch. 5 - RNA A. carbohydrate B. lipid C. protein D. nucleic...Ch. 5 - collagen A. carbohydrate B. lipid C. protein D....Ch. 5 - hemoglobin A. carbohydrate B. lipid C. protein D....Ch. 5 - A. carbohydrate B. lipid C. protein D. nucleic...Ch. 5 - Prob. 7TYKMCh. 5 - enzyme A. carbohydrate B. lipid C. protein D....Ch. 5 - cellulose A. carbohydrate B. lipid C. protein D....Ch. 5 - Chitin A. carbohydrate B. lipid C. protein D....Ch. 5 - Polymerization (the formation of polymers) is a...Ch. 5 - Which of the following statements is not true of a...Ch. 5 - Prob. 3TYKCh. 5 - Prob. 4TYKCh. 5 - Prob. 5TYKCh. 5 - Prob. 6TYKCh. 5 - A fatty acid that has the formula C16H32O2 is a....Ch. 5 - Prob. 8TYKCh. 5 - Prob. 9TYKCh. 5 - Prob. 10TYKCh. 5 - Which of the following molecules provides the most...Ch. 5 - Prob. 12TYKCh. 5 - What happens when a protein denatures? a. Its...Ch. 5 - The helix of proteins is a. part of a proteins...Ch. 5 - What is the best description of the following...Ch. 5 - Prob. 16TYKCh. 5 - Prob. 17TYKCh. 5 - Which of the following is true of the subunits of...Ch. 5 - Prob. 19TYKCh. 5 - If the nucleotide sequence of one strand of a DNA...Ch. 5 - How are nucleotide monomers connected to form a...Ch. 5 - Prob. 22TYK
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
- Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternaryarrow_forwardHow would adding acid to a non-buffered solution be most likely to affect protein structure? Select one: a. Adding acid would disrupt the primary structure of the protein b. Adding acid would cause the protein to become a lipid c. Adding acid would cause the protein to become a carbohydrate d. Adding acid would disrupt the secondary and tertiary structure of the proteinarrow_forwardWhat is the general characteristic of protein domains? A. All protein domains exhibit both a and B structures B. Protein domains constitute supersecondary structures that have specific biological functions in proteins. C. Most protein domains can be hydrolyzed from parent polypeptide chains while retaining functions and/or structures that are conserved. D. Protein domains constitute the structural block from which the protein is built E. Protein domains contain motifs that are the binding sites for prosthetic groups such as heme, or the iron-sulfur clusters.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 is true when speaking about the secondary structure of a protein A. invoves R group binding b. involves binding to other protiens c. involves hydrogen bonding of the protien backbone d. involves peptide bindingarrow_forwardThe difference between a polypeptide and a protein is a. that proteins are polypeptides folded up into a functional three-dimensional conformation b. that proteins are precursors of polypeptides c. that polypeptides are made of protein folded up into a functional three-dimensional conformation d. that proteins are always made with many polypeptidesarrow_forward
- 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 interactionsarrow_forwardWhich of the following might cause the denaturation of a protein? Select all that apply. A.)Highly acidic conditions B.)Highly basic conditions C.)High concentrations of salt D.)High heatarrow_forwardWhich of the following is NOT an example of protein secondary structure? a. alpha-helix b. beta sheets c. beta turn d. coiled coil e. loopsarrow_forward
- Which of the following types of molecular interactions play a role in protein folding? Select all that apply. A.)Hydrophobic interactions B.)Van der Waals attraction C.)Hydrogen bonds D.)Covalent bondsarrow_forwardWhich type of amino acid would you expect to find in large numbers in a protein found in a deep-sea hydrothermal vent (a very hot environment)? A.)Polar amino acids B.)Cysteines C.)Hydrophobic amino acids D.)Nonpolar amino acidsarrow_forwardWhich statement(s) correctly describe(s) protein structures?A. All hydrophobic residues are buried when protein structures and protein aggregatesB. Charged and polar amino acid residues are seldom buried in the protein interior C. Lysine is found only in the protein interiorD. Glycine is rarely found in proteins due to its destabilizing effect A,B,C A,C B B,C,Darrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Human Biology (MindTap Course List)BiologyISBN:9781305112100Author:Cecie Starr, Beverly McMillanPublisher:Cengage LearningBiology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher:Cengage Learning
Human Biology (MindTap Course List)
Biology
ISBN:9781305112100
Author:Cecie Starr, Beverly McMillan
Publisher:Cengage Learning
Biology (MindTap Course List)
Biology
ISBN:9781337392938
Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
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