Essentials of Biology (5th International Edition)
5th Edition
ISBN: 9781259660269
Author: Sylvia S. Mader, Dr., Michael Windelspecht
Publisher: Mcgraw-Hill
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 5, Problem S3.2BYB
Section 3.2 What are the four levels of structure associated with the three-dimensional shape of a protein?
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
What is the Three-Dimensional Structure of a Protein’s Amino Acid Sequence Dictates?
What level of protein structure is determined by the following:(a) Peptide bonds between amino acids?(b) Hydrogen bonds between backbone carbonyl oxygen atoms and hydrogen atoms attached to backbone nitrogen atoms?(c) R group interactions that may involve Van der Waalsforces, ionic interactions, or hydrogen bonds?
Protein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct?
1) the folding pattern of a protein is ultimately determined by its amino acid sequence.
2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface.
3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains.
4) the overall folding pattern/shape of a protein molecule is termed its primary structure.
5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence.
More than one answer might be right
Chapter 5 Solutions
Essentials of Biology (5th International Edition)
Ch. 5.1 - Prob. 5.1LOCh. 5.1 - Prob. 1LOCh. 5.1 - Prob. 2LOCh. 5.1 - Prob. 3LOCh. 5.1 - Prob. 1CYPCh. 5.1 - Prob. 2CYPCh. 5.1 - Prob. 3CYPCh. 5.1 - Prob. 1ACh. 5.1 - Prob. 2ACh. 5.1 - Prob. 3A
Ch. 5.2 - Prob. 1LOCh. 5.2 - Prob. 2LOCh. 5.2 - Prob. 3LOCh. 5.2 - Prob. 1CYPCh. 5.2 - Prob. 2CYPCh. 5.2 - Prob. 3CYPCh. 5.2 - Identify the incorrect statement a. When ATP...Ch. 5.2 - Prob. 5ACh. 5.3 - Illustrate how metabolic reactions are catalyzed...Ch. 5.3 - Identify the role that enzymes play in metabolic...Ch. 5.3 - Prob. 3LOCh. 5.3 - Prob. 4LOCh. 5.3 - Prob. 5LOCh. 5.3 - Prob. 1CYPCh. 5.3 - Prob. 2CYPCh. 5.3 - Summarize the benefit of using feedback inhibition...Ch. 5.3 - 6. In the induced fit model of enzyme action,
a....Ch. 5.3 - Prob. 7ACh. 5.3 - Prob. 8ACh. 5.4 - Prob. 1LOCh. 5.4 - Prob. 2LOCh. 5.4 - Prob. 3LOCh. 5.4 - Prob. 4LOCh. 5.4 - Prob. 5LOCh. 5.4 - Prob. 1CYPCh. 5.4 - Prob. 2CYPCh. 5.4 - Prob. 3CYPCh. 5.4 - Prob. 4CYPCh. 5.4 - Prob. 9ACh. 5.4 - Prob. 10ACh. 5.4 - Match the items to the correct answers in the key....Ch. 5.4 - Prob. 12ACh. 5.4 - Prob. 13ACh. 5.4 - Prob. 14ACh. 5.4 - Prob. 15ACh. 5 - Prob. 1BYBCh. 5 - Prob. 2BYBCh. 5 - Prob. S1.1BYBCh. 5 - Section 3.2 What are the four levels of structure...Ch. 5 - Prob. S4.2BYBCh. 5 - Prob. 1TCCh. 5 - Cystic fibrosis is a genetic disorder that results...Ch. 5 - Prob. 3TC
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
- How do the following interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.(a) Side-chain hydrogen bonding(b) Disulfide bondsarrow_forwardWhat is the importance of each protein structure (Primary, Secondary, Tertiary, and Quaternary structure)?arrow_forwardWhat are the major properties that distinguish different amino acids from one another? What roles do these differences play in the structure and function of proteins?arrow_forward
- what are the four interactions that keep the protein structure intact?arrow_forwardIdentify 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_forwardWhat are the four levels of protein structure, and what is the distinguishing feature of each?arrow_forward
- What are the four levels of protein structure, and what is the distinguishing feature of each?arrow_forwardWhich of the following amino acids is most likely to be found on the outside of a soluble protein, and which of them is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acidside chain in each case and that the protein is folded up into its globular form.)(a) Valine (b) Aspartate(c) Histidine (d) Alaninearrow_forwardWhat is the key structural difference between fibrous and globular proteins? How is it related, in general, to the proteins’amino acid composition?arrow_forward
- What primarily determines the secondary and tertiary structures of a protein?arrow_forwardWhich of the following amino acids is most likely to be found on the outside of a soluble protein? Which is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acid side chain in each case and that the protein is folded up into its globularform.)(a) Leucine (b) Glutamate(c) Phenylalanine (d) Glutaminearrow_forwardwhat are the four levels of protein structure? what stabilizes each level of folding? what environmental factors affect protein folding?arrow_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
Macromolecules | Classes and Functions; Author: 2 Minute Classroom;https://www.youtube.com/watch?v=V5hhrDFo8Vk;License: Standard youtube license