Biology
12th Edition
ISBN: 9781260494570
Author: Raven, Peter
Publisher: MCGRAW-HILL HIGHER EDUCATION
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Textbook Question
Chapter 3, Problem 4A
A mutation that alters a single amino acid within a protein can alter
a. the primary level of protein structure.
b. the secondary level of protein structure.
c. the tertiary level of protein structure.
d. All of the choices are correct.
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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.
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
In a protein, a mutation occurs and results in phenylalanine being replaced by an alanine. This would.
Select one:
a. Always change the primary structure of the protein, never change the tertiary structure of function.
O b. Always change the primary structure of a protein, sometimes affect tertiary structure and function.
c Never change the primary structure, always affect secondary and tertiary structure and function.
O d. Sometimes change the primary structure of a protein, always affect the tertiary structure, and sometimes affect
function.
Chapter 3 Solutions
Biology
Ch. 3.1 - Describe the relationship between functional...Ch. 3.1 - Recognize the different kinds of isomers.Ch. 3.1 - Prob. 3LOCh. 3.2 - Prob. 1LOCh. 3.2 - Prob. 2LOCh. 3.3 - Prob. 1LOCh. 3.3 - Prob. 2LOCh. 3.3 - Prob. 3LOCh. 3.3 - Prob. 4LOCh. 3.4 - Prob. 1LO
Ch. 3.4 - Prob. 2LOCh. 3.4 - Prob. 3LOCh. 3.5 - Prob. 1LOCh. 3.5 - Prob. 2LOCh. 3.5 - Prob. 3LOCh. 3 - Prob. 1UCh. 3 - Why are carbohydrates important molecules for...Ch. 3 - Plant cells store energy in the form of ______,...Ch. 3 - Prob. 4UCh. 3 - A molecule of DNA or RNA is a polymer of a....Ch. 3 - Prob. 6UCh. 3 - What monomers make up a protein? a....Ch. 3 - A triglyceride is a form of _______ composed of...Ch. 3 - You can use starch or glycogen as an energy...Ch. 3 - Which of the following is NOT a difference between...Ch. 3 - Prob. 3ACh. 3 - A mutation that alters a single amino acid within...Ch. 3 - Two different proteins have the same domain in...Ch. 3 - What aspect of triglyceride structure accounts for...Ch. 3 - The spontaneous formation of a lipid bilayer in an...Ch. 3 - Prob. 1SCh. 3 - Hydrogen bonds and hydrophobic interactions each...Ch. 3 - Prob. 3S
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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
- 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 FALSE? Select one: a. Secondary structure of a protein determines how it folds up into a unique three dimensional structure. b. Three dimensional structure of a protein determines the function of a protein. c. Primary structure of a protein determines how it folds up into a unique three dimensional structure. d. Amino acid sequence is absolutely important for a particular protein.arrow_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_forward
- 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_forwardA prosthetic group of a protein is a non-protein structure that is: a. a ligand of the protein. b. a part of the secondary structure of the protein. c. a substrate of the protein. d. permanently (tightly) associated with the protein. e. transiently bound to the protein.arrow_forwardProteins often have regions that show specific, coherent patterns of folding or function. These regions are called: a. domains. b.oligomers. c. peptides. d. sites. e. subunits.arrow_forward
- Which of the following is the smallest amino acid?* Please choose one correct answer only. A. G B. A C. P D. W E. Darrow_forwardIn order to study protein structures and functions, many protein techniques have been developed for specific applications. Which of the following pair of technique: application is INCORRECT? a. Mass Spectrometry: protein molecular weight b. SDS-PAGE: protein structure c. X-ray crystallography: protein structure d. NMR: protein structure e. Peptide mass fingerprinting: protein presence and identificationarrow_forwardTwo amino acids of the standard 20 contain sulfur atoms. They are: a. cysteine and serine. b. cysteine and threonine. c. methionine and cysteine d. methionine and serine e. threonine and serine.arrow_forward
- The 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_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_forwardWhich 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_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY