Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 10, Problem 44RE
Interpretation Introduction
Interpretation:
The reason behind the fact that nonhomologous end joining is an error-prone mechanism is to be explained.
Concept introduction:
The preservation of the DNA (deoxyribonucleic acid) double helix integrity is very important for the maintenance of genomic stability. The breaks in double-stranded DNA represent a great threat to the cells.
There are two mechanisms to repair the double-stranded breaks in the DNA—homologous and nonhomologous end joining.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Why don’t we see amino acids with certain properties (e.g., a straight-chain side chain with two carbons, multiple hydroxyl groups, or other unusual structures)?
Please analze the gel electrophoresis column of the VRK1 kinase (MW: 39.71 kDa).
Lane 1: buffer
Lane 2 : Ladder
Lane 3: Lysate
Lane 4: Flowthrough
Lane 5: Wash
Lanes 6-8: E1, E2, E3
Lane 9: Dialyzed VRK1
Lane 10: LDH
Please help
Chapter 10 Solutions
Biochemistry
Ch. 10 - RECALL Define replication, transcription, and...Ch. 10 - REFLECT AND APPLY Is the following statement true...Ch. 10 - REFLECT AND APPLY Why is it more important for DNA...Ch. 10 - RECALL Why is the replication of DNA referred to...Ch. 10 - RECALL What is a replication fork? Why is it...Ch. 10 - Prob. 6RECh. 10 - RECALL Why is it necessary to unwind the DNA helix...Ch. 10 - REFLECT AND APPLY In the MeselsonStahl experiment...Ch. 10 - REFLECT AND APPLY Suggest a reason why it would be...Ch. 10 - RECALL Do DNA-polymerase enzymes also function as...
Ch. 10 - RECALL Compare and contrast the properties of the...Ch. 10 - REFLECT AND APPLY Define processivity, and...Ch. 10 - REFLECT AND APPLY Comment on the dual role of the...Ch. 10 - REFLECT AND APPLY What is the importance of...Ch. 10 - REFLECT AND APPLY DNA synthesis always takes place...Ch. 10 - REFLECT AND APPLY What would happen to the...Ch. 10 - Prob. 17RECh. 10 - REFLECT AND APPLY Why is it not surprising that...Ch. 10 - Prob. 19RECh. 10 - RECALL List the substances required for...Ch. 10 - RECALL Describe the discontinuous synthesis of the...Ch. 10 - RECALL What are the functions of the gyrase,...Ch. 10 - RECALL Single-stranded regions of DNA are attacked...Ch. 10 - RECALL Describe the role of DNA ligase in the...Ch. 10 - RECALL What is the primer in DNA replication?Ch. 10 - Prob. 26RECh. 10 - REFLECT AND APPLY Why is a short RNA primer needed...Ch. 10 - Prob. 28RECh. 10 - RECALL What was the recent change in the estimated...Ch. 10 - Prob. 30RECh. 10 - RECALL Why is a clamp loader necessary in...Ch. 10 - RECALL How does proofreading take place in the...Ch. 10 - Prob. 33RECh. 10 - Prob. 34RECh. 10 - BIOCHEMICAL CONNECTIONS Of what benefit is it for...Ch. 10 - REFLECT AND APPLY Your book contains about 2...Ch. 10 - REFLECT AND APPLY E. coli incorporates...Ch. 10 - REFLECT AND APPLY Given the typing speed from...Ch. 10 - Prob. 39RECh. 10 - REFLECT AND APPLY How can breakdown in DNA repair...Ch. 10 - Prob. 41RECh. 10 - RECALL What is a direct way of repairing...Ch. 10 - Prob. 43RECh. 10 - Prob. 44RECh. 10 - Prob. 45RECh. 10 - Prob. 46RECh. 10 - RECALL How did Messelson and Weigle demonstrate...Ch. 10 - Prob. 48RECh. 10 - RECALL What is the Holliday Model?Ch. 10 - RECALL Do eukaryotes have fewer origins of...Ch. 10 - RECALL How does DNA replication in eukaryotes...Ch. 10 - Prob. 52RECh. 10 - REFLECT AND APPLY (a) Eukaryotic DNA replication...Ch. 10 - Prob. 54RECh. 10 - Prob. 55RECh. 10 - Prob. 56RECh. 10 - Prob. 57RECh. 10 - Prob. 58RECh. 10 - Prob. 59RECh. 10 - Prob. 60RECh. 10 - Prob. 61RECh. 10 - Prob. 62RECh. 10 - Prob. 63RECh. 10 - Prob. 64RE
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
- 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.arrow_forwardIn 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 youarrow_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. 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_forward
- Three 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_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. 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_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. 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_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. 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_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. 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_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY