Human Physiology
15th Edition
ISBN: 9781259864629
Author: Fox, Stuart Ira
Publisher: Mcgraw-hill Education,
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Textbook Question
Chapter 2, Problem 10RA
The tertiary structure of a protein is directly determined by
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Which 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.
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.
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.
Chapter 2 Solutions
Human Physiology
Ch. 2 - List the components of an atom and explain how...Ch. 2 - Describe the nature of nonpolar and polar covalent...Ch. 2 - Define the terms acidic, basic, acid, and base....Ch. 2 - Using chemical equations, explain how bicarbonate...Ch. 2 - Prob. 4CPCh. 2 - Describe the structural characteristic of all...Ch. 2 - Describe the characteristics of a lipid, and...Ch. 2 - Explain, in terms of dehydration synthesis and...Ch. 2 - Relate the functions of phospholipids to their...Ch. 2 - Write the general formula for an amino acid, and...
Ch. 2 - Describe and account for the different levels of...Ch. 2 - Describe the different categories of protein...Ch. 2 - Prob. 10aCPCh. 2 - Prob. 10bCPCh. 2 - Describe the structure of DNA, and explain the law...Ch. 2 - Which of these statements about atoms is true?...Ch. 2 - The bond between oxygen and hydrogen in a water...Ch. 2 - Which of these is a nonpolar covalent bond?...Ch. 2 - Solution A has a pH of 2, and solution B has a pH...Ch. 2 - Glucose is
Ch. 2 - Digestion reactions occur by means of...Ch. 2 - Carbohydrates are stored in the liver and muscles...Ch. 2 - Lecithin is
Ch. 2 - Which of these Lipids have regulatory roles in the...Ch. 2 - The tertiary structure of a protein is directly...Ch. 2 - The type of bond formed between two molecules of...Ch. 2 - The carbon-to-nitrogen bond that joins amino acids...Ch. 2 - Prob. 13RACh. 2 - Prob. 14RACh. 2 - Prob. 15RACh. 2 - Prob. 16RACh. 2 - Prob. 17RACh. 2 - Explain, in terms of dehydration synthesis and...Ch. 2 - Prob. 19RACh. 2 - Prob. 20RACh. 2 - Explain how one DNA molecule serves as a template...Ch. 2 - Prob. 22RACh. 2 - Prob. 23RACh. 2 - From the ingredients listed on a food wrapper, it...Ch. 2 - Prob. 25RACh. 2 - Prob. 26RACh. 2 - Prob. 27RACh. 2 - Prob. 28RACh. 2 - Prob. 29RACh. 2 - The molecular weight is the sum of the atomic...
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- 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_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_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_forward
- Proteins 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_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_forwardWhich of the following describes the tertiary structure of proteins? A. Helices and sheets formed from hydrogen bonds between the amino acids of polypeptides B. The functional domains that form from interactions between different parts of the polypeptide C. The association of multiple polypeptides D. The linear sequence of amino acids making up the polypeptidearrow_forward
- 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.arrow_forwardWhich 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 acidsarrow_forwardWhich of the following describes a purpose of the glycosylation of proteins? A. Glycosylation tags a protein for destruction within a cell. B. Glycosylation is a process that causes cells to import new proteins from the extracellular space. C. Glycosylation indicates where a protein belongs within a cell. D. Glycosylation is the process of bonding amino acids to each other to build a protein.arrow_forward
- 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_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_forwardWhich of the following is a drawback of using base hydrolysis during amino acid composition? A. Protonation of basic amino acids. B. Dissociation of acidic amino acids. C. Denaturation of the protein. D. Racemization of certain amino acids.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