Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
8th Edition
ISBN: 9780134015187
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 23.7, Problem 23.20KCP
Interpretation Introduction
Interpretation:
The different composition of inner and outer surface has to be explained. And the use of different compositions has to be written.
Concept Introduction:
Cell membrane:
The cell membrane it is a fluid mosaic, the semi-permeable membrane surrounding the cytoplasm of a cell it is flexible and made up of different type of molecules.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Please help
You have isolated a protein and determined that the native molecular weight of the holoenzyme is 160 kD using size exclusion chromatography. Analysis of this protein using SDS-PAGE revealed 2 bands, one at 100 kD and one at 30 kD.
Describe the architecture of the polypeptide component of this enzyme.
In a cell free preparation of beta-lactamase, penicillin is hydrolyzed in a D2O enriched assay. After one round of catalysis, where would you anticipate finding Deuterium?
please help thank you
Chapter 23 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
Ch. 23.1 - Use Figure 23.1 to identify the family of lipids...Ch. 23.2 - Prob. 23.2PCh. 23.2 - Prob. 23.3PCh. 23.2 - Prob. 23.4KCPCh. 23.3 - Prob. 23.1CIAPCh. 23.3 - Prob. 23.2CIAPCh. 23.3 - Prob. 23.3CIAPCh. 23.3 - Prob. 23.5PCh. 23.3 - Prob. 23.6PCh. 23.3 - Prob. 23.7KCP
Ch. 23.4 - Prob. 23.8PCh. 23.4 - Prob. 23.9PCh. 23.4 - Prob. 23.10PCh. 23.4 - Prob. 23.11PCh. 23.5 - Prob. 23.12PCh. 23.5 - Draw the structure of the sphingomyelin that...Ch. 23.5 - Draw the structure of the glycerophospholipid that...Ch. 23.5 - Prob. 23.16PCh. 23.7 - Prob. 23.17KCPCh. 23.7 - Prob. 23.4CIAPCh. 23.7 - Prob. 23.6CIAPCh. 23.7 - Prob. 23.7CIAPCh. 23.7 - Prob. 23.8CIAPCh. 23.7 - Prob. 23.18PCh. 23.7 - Prob. 23.19PCh. 23.7 - Prob. 23.20KCPCh. 23 - The fatty acid composition of three...Ch. 23 - Prob. 23.23UKCCh. 23 - According to the fluid-mosaic model (Figure 23.7),...Ch. 23 - Dipalmitoylphosphatidylcholine (DPPC) is a...Ch. 23 - Prob. 23.26APCh. 23 - Prob. 23.27APCh. 23 - Prob. 23.28APCh. 23 - Prob. 23.29APCh. 23 - Differentiate between saturated, monounsaturated,...Ch. 23 - Are the carboncarbon double bonds in naturally...Ch. 23 - Prob. 23.32APCh. 23 - Prob. 23.33APCh. 23 - Which of these fatty acids has the lower melting...Ch. 23 - Which of these fatty acids has the higher melting...Ch. 23 - Prob. 23.36APCh. 23 - Prob. 23.37APCh. 23 - Prob. 23.38APCh. 23 - Prob. 23.39APCh. 23 - What function does a wax serve in a plant or...Ch. 23 - Prob. 23.41APCh. 23 - Prob. 23.42APCh. 23 - What kind of lipid is spermacetia fat, a wax, or a...Ch. 23 - Prob. 23.44APCh. 23 - Prob. 23.45APCh. 23 - Prob. 23.46APCh. 23 - Prob. 23.47APCh. 23 - Prob. 23.48APCh. 23 - Prob. 23.50APCh. 23 - Prob. 23.52APCh. 23 - Prob. 23.53APCh. 23 - Describe the difference between a triacylglycerol...Ch. 23 - Why are glycerophospholipids, rather than...Ch. 23 - Prob. 23.56APCh. 23 - Prob. 23.57APCh. 23 - Why are glycerophospholipids more soluble in water...Ch. 23 - Prob. 23.59APCh. 23 - Prob. 23.60APCh. 23 - Prob. 23.61APCh. 23 - Draw the structure of a glycerophospholipid that...Ch. 23 - Prob. 23.63APCh. 23 - What is a major function of cholesterol in your...Ch. 23 - Prob. 23.65APCh. 23 - Prob. 23.66APCh. 23 - Prob. 23.67APCh. 23 - Explain how a micelle differs from a membrane...Ch. 23 - Prob. 23.69APCh. 23 - Prob. 23.70APCh. 23 - Prob. 23.71APCh. 23 - Prob. 23.72APCh. 23 - Prob. 23.73APCh. 23 - Prob. 23.74APCh. 23 - Prob. 23.75APCh. 23 - Draw the structure of a triacylglycerol made from...Ch. 23 - Prob. 23.79CPCh. 23 - Prob. 23.80CPCh. 23 - Explain why cholesterol is not saponifiable.Ch. 23 - Draw cholesterol acetate. Is this molecule...Ch. 23 - Prob. 23.83CPCh. 23 - Prob. 23.84CPCh. 23 - Prob. 23.85CPCh. 23 - Prob. 23.86CPCh. 23 - Prob. 23.88GP
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- To map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. question: the b-lactamase hydrolyzes the lactam-ring in antibiotics like penicillin. Describe the mechanism, of hydrolysis, insuring to include the involvement of S, D, and K in the reaction sequence. Please help!arrow_forwardThree of these amino acids participate in the proteolytic hydrolysis of polypeptides. Show the charge-relay network generated by the serine proteases and identify the nucleophilic species that initiates the hydrolysis. please help!arrow_forwardYou have isolated a protein and determined that the native molecular weight of the holoenzyme is 160 kD using size exclusion chromatography. Analysis of this protein using SDS-PAGE revealed 2 bands, one at 100 kD and one at 30 kD. 1. Describe the architecture of the polypeptide component of this enzyme. 2. The enzyme was found to be 0.829% NAD (by weight). What further can be said regarding the architecture? can you please help me with question number 2arrow_forward
- To map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Question: although S, K, and D are involved in the catalysis, the E in this hexapeptide does not participate in the hydrolysis of the b-lactam ring. Why is that?arrow_forwardTo map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. a) Using the experimental results described below deduce the primary sequence of the active site hexapeptide. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. please help!arrow_forwardThe beta-lactamase hydrolyzes the lactam-ring in penicillin. Describe the mechanism of hydrolysis, insuring to include the involvement of S, D, & K in the reaction sequence. Please helparrow_forward
- To map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Why doesn't D in this hexapeptide not participate in the hydrolysis of the beta-lactam ring even though S, K, and D are involved in the catalyst?arrow_forwardTo map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Using the experimental results described above derive the primary sequence of the active site hexapeptide. Please help!arrow_forwardWhich type of enzyme catalyses the following reaction? oxidoreductase, transferase, hydrolase, lyase, isomerase, or ligase.arrow_forward
- +NH+ CO₂ +P H₂N + ATP H₂N NH₂ +ADParrow_forwardWhich type of enzyme catalyses the following reaction? oxidoreductase, transferase, hydrolase, lyase, isomerase, or ligase.arrow_forwardWhich features of the curves in Figure 30-2 indicates that the enzyme is not consumed in the overall reaction? ES is lower in energy that E + S and EP is lower in energy than E + P. What does this tell you about the stability of ES versus E + S and EP versus E + P.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Biology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax
Concepts of BiologyBiologyISBN:9781938168116Author:Samantha Fowler, Rebecca Roush, James WisePublisher:OpenStax College
Biology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher:Cengage Learning
Human Biology (MindTap Course List)BiologyISBN:9781305112100Author:Cecie Starr, Beverly McMillanPublisher:Cengage Learning
Biology Today and Tomorrow without Physiology (Mi...BiologyISBN:9781305117396Author:Cecie Starr, Christine Evers, Lisa StarrPublisher:Cengage Learning
Human Physiology: From Cells to Systems (MindTap ...BiologyISBN:9781285866932Author:Lauralee SherwoodPublisher:Cengage Learning
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Concepts of Biology
Biology
ISBN:9781938168116
Author:Samantha Fowler, Rebecca Roush, James Wise
Publisher:OpenStax College
Biology (MindTap Course List)
Biology
ISBN:9781337392938
Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher:Cengage Learning
Human Biology (MindTap Course List)
Biology
ISBN:9781305112100
Author:Cecie Starr, Beverly McMillan
Publisher:Cengage Learning
Biology Today and Tomorrow without Physiology (Mi...
Biology
ISBN:9781305117396
Author:Cecie Starr, Christine Evers, Lisa Starr
Publisher:Cengage Learning
Human Physiology: From Cells to Systems (MindTap ...
Biology
ISBN:9781285866932
Author:Lauralee Sherwood
Publisher:Cengage Learning
Macromolecules | Classes and Functions; Author: 2 Minute Classroom;https://www.youtube.com/watch?v=V5hhrDFo8Vk;License: Standard youtube license