Biological Science (7th Edition)
7th Edition
ISBN: 9780134678320
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Greg Podgorski, Emily Taylor, Jeff Carmichael
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 3, Problem 12PIAT
Summary Introduction
Introduction:
Normally when you eat food, the digestive enzymes break down proteins into their respective amino acids and these amino acids are further converted into short strings of amino acids called peptides. Glutens are resistant to digestion in the small intestine and sometimes peptides disrupt the lining of the small intestine.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Side chains of which two amino acids may participate in peptide bonding?
A. Alanine and Glycine
B. Phenylalanine and Tryptophan
OC. Histidine and Tyrosine
D. Glutamic acid and Lysine
E. Leucine and Isoleucine
Consider the following situation; Fresh pineapple contains the enzyme bromelain that hydrolyzes peptide bonds in proteins.
a. The directions in making a gelatin (protein) dessert say not to add fresh pineapple. However, canned pineapple where pineapple is heated to high temperatures can be added. Why?
b. Fresh pineapple is used in a marinade to tenderize tough meat. Why?
c. What structural level of a protein does the bromelain enzyme destroy?
A histidine was determined to be the critical residue involved in an enzyme-catalyzed reaction. If the pKa of the histidine is known to be 6.5 in the active site and the pH of maximum catalytic activity is 7.2, what is likely the primary role of histidine in the catalytic reaction?
A. forms a covalent bond with the substrate
B. reduces the entropy of the substrate
C. stabilizes a charged intermediate
D. acts as a proton donor
Aspartate and lysine are in the active site of an enzyme. They are both known to participate directly in catalysis. The pKa's of the residues are found to be 3.2 and 9.6, respectively for aspartate and lysine. The optimum pH for the enzyme is 6.4. Which forms of these two residues will predominate when the enzyme is most active?
A. aspartate is protonated; lysine is deprotonated
B. both residues are deprotonated
C. aspartate is deprotonated; lysine is protonated
D. both residues are protonated
Chapter 3 Solutions
Biological Science (7th Edition)
Ch. 3 - 1. What two functional groups are bound to the...Ch. 3 - What type of information is used to direct...Ch. 3 - Prob. 5TYUCh. 3 - Prob. 6TYUCh. 3 - 7. Why are proteins not considered to be a good...Ch. 3 - Prob. 9TYPSSCh. 3 - Prob. 12PIATCh. 3 - Prob. 13PIATCh. 3 - Recall that proline often introduces kinks in the...Ch. 3 - SOCIETY Based on the experiment in question 15,...
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
- You are studying Protein X, which is a tetramer whose function is to bind glucose. You have found a molecule that is an allosteric effector of the protein’s activity. This means that: a. The molecule causes Protein X to bind O2 very tightly b. The molecule does not bind in the active site but affects the function of the protein c. The molecule is highly negatively charged d. The molecule binds in the same site as glucosearrow_forwardUse drawings to explain how an enzyme (such as hexokinase, mentioned in the text) can distinguish its normal substrate (here d-glucose) from the optical isomer l-glucose, which is not a substrate. (hint: remembering that a carbon atom forms four single bonds that are tetrahedrally arranged and that the optical isomers are mirror images of each other around such a bond, draw the substrate as a simple tetrahedron with four different corners and then draw its mirror image. using this drawing, indicate why only one optical isomer might bind to a schematic active site of an enzyme.)arrow_forwardRefer to image below: Identify the R-group of each molecule. * H3C. OH HS OH H2N. HO. ČH3 NH2 NH2 NH2 Choose A. Alkyl B. Sulfide C. Guanidino A. Alkyl B. Thiol C. Amino A. Ethylene B. Thiol C. Amino A. Alkyl B. Sulfide C. Amino nino acids. *arrow_forward
- Liver and other organ meats contain large quantities of nucleic acids. In the course of digestion, RNA is hydrolyzed to ribose, among other chemicals. Explain how ribose can be used as a fuel.arrow_forwardAcid hydrolysis of proteins in order to determine the amino acid composition leaves most of the amino acid residues intact but: O a. converts asparagine to aspartic acid O b.oxidizes leucine to isoleucine O c. destroys glutamic and aspartic acid O d. destroys the basic amino acids O e. destroys prolinearrow_forwardThe pKa of the protonated, positively charged form of the side chain of histidine is approximately 6. In a solution with a pH of 8, the side chain of histidine is most likely to be: A. twice protonated and charged. B. once protonated and uncharged. C. completely deprotonated and charged. D. once protonated and charged.arrow_forward
- Which of the following describes lactose? A. A nonreducing disaccharide containing glucose and fructose linked by a (α1-->4) bond. B. A reducing disaccharide containing two glucose molecules linked by a (α1-->4) bond. C. A reducing disaccharide containing two glucose molecules linked by a (β1-->4) bond. D. A reducing disaccharide containing galactose and glucose linked by a (β1-->4) bond. E. A nonreducing disaccharide containing galactose and glucose linked by a (α1-->4) bond.arrow_forwardThe storage polysaccharide starch is a mixture of the molecules amylose (an unbranched polymer of glucose) and amylopectin (a branched polymer of glucose). Both amylose and amylopectin only have one reducing end, but amylopectin has many nonreducing ends.Enzymes that break down these molecules act on the nonreducing ends. Briefly describe why this is advantageous.arrow_forwardWhich of the following is incorrect? a. Asp and Glu are basic amino acids b. Asp and Glu are (-) charged at pH 7 Oc. The side chains of Asp and Glu have a pk of about 4 C. d. The side chain of His has a pK of about 6arrow_forward
- Gd(III) needs to be strongly chelated when used in medical imaging applications because the free ion can displace Ca(I) in protein active sites and disrupt biological function. What is the best atom to Coordinate these metal ions from amino acids? A. Oxygen B. Nitrogen C. Sulfur D. Carbonarrow_forwardDraw the functional portion of the cofactor/pro and explain the functional role in each reaction.arrow_forwardIdentify which of the following pairs of amino acid residues can have hydrogen bonding between their side chains. A. Alaine and Glycine B. Leucine and Isoleucine C. Valinc and Asparaginc D. Threonine and Tryrosinearrow_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