Campbell Biology In Focus
2nd Edition
ISBN: 9780134203072
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 3, Problem 6TYU
The structural level of a protein least a fleeted by a disruption in hydrogen bonding is the
- A. primary level.
- B. secondary level.
- C. tertiary level.
- D. quaternary level.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
The 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.
Denaturation 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.
Which 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.
Chapter 3 Solutions
Campbell Biology In Focus
Ch. 3.1 - How are gasoline and fat chemically similar?Ch. 3.1 - Which molecules in Figure 3.4a re isomers? For...Ch. 3.1 - Prob. 3CCCh. 3.1 - Prob. 4CCCh. 3.2 - How many molecules of water are needed to...Ch. 3.2 - WHAT IF? Suppose you eat a serving of fish. What...Ch. 3.3 - Write the formula for a monosaccharide that has...Ch. 3.3 - A dehydration reaction joins two glucose molecules...Ch. 3.3 - WHAT IF? After a cow is given antibiotics to treat...Ch. 3.4 - Compare the structure of a fat (triglyceride) with...
Ch. 3.4 - Why are human sex hormones considered lipids?Ch. 3.4 - Prob. 3CCCh. 3.5 - Why does a denatured protein no longer function...Ch. 3.5 - What parts of a polypeptide participate in the...Ch. 3.5 - WHAT IF? Where would you expect a polypeptide...Ch. 3.6 - DRAW IT Go to Figure 3.27a and, for the top three...Ch. 3.6 - Prob. 2CCCh. 3.7 - How would sequencing the entire genome of an...Ch. 3.7 - Given the function of DNA, why would you expect...Ch. 3 - Prob. 1TYUCh. 3 - Which functional group is not present in this...Ch. 3 - MAKE CONNECTIONS Which chemical group is most...Ch. 3 - Prob. 4TYUCh. 3 - Which of the following statements concerning...Ch. 3 - The structural level of a protein least a fleeted...Ch. 3 - Enzymes that break down DNA catalyze the...Ch. 3 - Prob. 8TYUCh. 3 - The molecular formula for glucose is C6H12O6. What...Ch. 3 - Construct a table that organizes the following...Ch. 3 - Prob. 11TYUCh. 3 - Prob. 12TYUCh. 3 - FOCUS ON ORGANIZATION Proteins, which have diverse...Ch. 3 - Prob. 14TYUCh. 3 - SYNTHESIZE YOUR KNOWLEDGE Given that the function...
Additional Science Textbook Solutions
Find more solutions based on key concepts
Match the people in column A to their contribution toward the advancement of microbiology, in column B. Column ...
Microbiology: An Introduction (13th Edition)
To test your knowledge, discuss the following topics with a study partner or in writing ideally from memory. Th...
Human Anatomy
Describe the role and impact of microbes on the earth.
Microbiology Fundamentals: A Clinical Approach - Standalone book
a. What three lineages of lobe-fins survive today? b. Go back to the phylogenetic tree in Interactive Question ...
Study Guide for Campbell Biology
Relative thickness of the myocardium in different chambers; the functional significance of those differences; a...
Anatomy & Physiology: The Unity of Form and Function
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
- The tertiary structure of a protein is established by: a. The sequence of amino acids in the protein b. The molecular weight of the protein c. The total number of amino acids in the protein d. The number of disulfide bridges in the protein e. The net charge of the the protein at physioloical pH.arrow_forwardMatch 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_forwardThe structure of a protein results from the folding ofthe pleated sheets or helices.a. primary c. tertiaryb. secondary d. quaternaryarrow_forward
- Variations in three-dimensional shapes among proteins are due tobonding between thea. amino groups.b. R groups.c. ion groups.d. H atomsarrow_forwardThis structure of a protein comes from the further bending and folding of pleated sheets and helices: A. primary B. secondary C. tertiary D. quaternaryarrow_forwardThe structural level of a protein least affected by a disruption in hydrogen bonding is the a. primary b.secondary c. tertiary d. quaternaryarrow_forward
- Large globular proteins frequently are comprised of two or more recognizable structures that often confer unique functions or properties. These structures are termed: a quatemary structure b. domains c. heterotropic d. multimeric e à andearrow_forwardAt what level(s) of protein structure would you expect to find disulfide bridges? a. primary O b. secondary O c. tertiary d. quaternary e. only in b and carrow_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
- A. A macromolecule composed of one or more polypeptides B. The monomer of polypeptides. C. The specific sequence of amino acids in a polypeptide. D. Structure of coils and/or folds of a polypeptide strueture. E. Structure of polypeptide resulting from interactions between R-groups. Contributes to unique 3D shape of molecule. F. Two or more polypeptides interacting to form a single functional unit. 1. Protein 2. amino acid 3. primary structure 4. secondary structure 5. tertiary structure 6. quaternary structurearrow_forwardWhich of the following bonding types is the most important in the nonaqueous interfaces between protein subunits? a. van der Waals interactions b. the hydrophobic effect c. ionic bonds d. disulfide bridgesarrow_forwardWhich 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_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Biology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher: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