Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN: 9781305389892
Author: Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher: Cengage Learning
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Chapter 3, Problem 15TYK
Summary Introduction
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The importance of the primary structure of proteins, in explaining evolutionary relationships.
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When comparing similarities among multiple protein structures, which of the following is false?
None of the above statements are false.
Proteins with the same function from different species are likely to be more similar in sequence than in
structure.
Proteins with the same function from a different species are likely to have similar motifs.
Proteins with the same motifs are likely to perform similar functions.
An effective protein motif is likely be observed in multiple proteins.
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A mutation leads to a change in amino acid from valine, an amino acid with a nonpolar side chain, to aspartic acid, an amino acid with a polar, negatively-charged side chain. Do you think that the following levels of protein structure change? If so, how and why? If not, why not? Please frame your answer in terms of chemical bonds and interactions. (primary structure, secondary structure, tertiary structure, quartenary structure)
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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
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- If an amino acid sequence is altered, could that affect a protein's tertiary structure? Why or why not? 1. No, because the amino acid sequence is not part of a protein 2. Yes, because the amino acid sequence determines how a protein folds 3. Yes, because the tertiary structure is the amino acid sequence 4. No, because the tertiary structure is the amino acid sequencearrow_forwardUsing what you have learned in protein structure, explain 4 ways that the alpha helix could contribute to tertiary structure.arrow_forwardwhich of the following is correct about the structure of proteins? a- the number of peptide bonds is equivalent to the number of amino acid residues b- the secondary structure of proteins are mostly stabilized by hydrophobic interactions c- protiens mostly composed of polar amino acids will have an elongated (fibrous) tertiary structure d- the quaternary structure of a protein is formed between or among similar polypeptides onlyarrow_forward
- The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are: a. always side by side. b. generally near each other in sequence. c. invariably restricted to about 7 of the 20 standard amino acids. d. often on different polypeptide strands. e. usually near the polypeptide chain's amino terminus or carboxyl terminus.arrow_forwardYou put albumin, the protein responsible for lipid transport through the blood, in methane, a hydrophobic solution. Would you expect albumin to still be functional? Yes the protein would still be functional because its primary structure remains intact Yes the protein would still be functional because it is used to carry lipids No the protein would not be functional because the peptide bonds would be dehydrated No the protein would not be functional because covalent bonds weaken and disrupt secondary structure No the protein would not be functional because the tertiary structure would change to maximize hydrophobic interactionsarrow_forwardWhich of the following statments are correct about protein evolution (select all that apply)? A. Most proteins only contain one structural domain B. Most naturally occurring mutations in a protein domain will substantially disrupt the structure C. Many individual doamins contain specialized functions that may be swapped between proteins D. It is the cummulative effects of mutations in a domain that lead to new structures and functions. E. Only mixing and matching of domains allow proteins to create new structuresarrow_forward
- 1. Is there more than one way to fold a protein, given the conflicting demands of the different "R" groups and the protein existing in a watery environment? 2. Explain what an R group is. 3. Compare the backbone of a polypeptide with that of a nucleic acid. 4. Proteins perform critical functions in all of our cells. Without proteins, life wouldn’t exist. Think of some specific proteins and describe what function they perform. 5. Explain the difference between secondary and tertiary protein structures.arrow_forwardProteins, the building blocks of life, have several functions in the human body and all the operations depend upon the structural specificity which can be explained by the lock and key hypothesis. Expand the ideaarrow_forwardA. 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_forward
- 1. How are organic molecules related to all living things?Explain. 2. Draw an Illustration showing the functions of protein in the body.arrow_forwardExplain what the protein folding problem is and why it is so difficult to predict protein structures from just their primary sequence. Highlight some of the specific challenges with your knowledge of protein secondary and tertiary structures. How would artificial intelligence or machine learning help with the de novo prediction of protein structures in the near future?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_forward
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