Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 13, Problem 15RE
RECALL What vectors can be used for cloning?
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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
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.
Chapter 13 Solutions
Biochemistry
Ch. 13 - RECALL What advantages does fluorescent labeling...Ch. 13 - RECALL What methods are used to visualize...Ch. 13 - REFLECT AND APPLY When proteins are separated...Ch. 13 - RECALL How does the use of restriction...Ch. 13 - RECALL What is the importance of methylation in...Ch. 13 - RECALL Why do restriction endonucleases not...Ch. 13 - Prob. 7RECh. 13 - Prob. 8RECh. 13 - RECALL What do the following have in common? MOM;...Ch. 13 - RECALL Give three examples of DNA palindromes.
Ch. 13 - RECALL What are three differences between the...Ch. 13 - RECALL What are sticky ends? What is their...Ch. 13 - RECALL What would be an advantage of using HaeIII...Ch. 13 - RECALL Describe the cloning of DNA.Ch. 13 - RECALL What vectors can be used for cloning?Ch. 13 - RECALL Describe the method you would use to test...Ch. 13 - RECALL What is blue/white screening? What is the...Ch. 13 - Prob. 18RECh. 13 - Prob. 19RECh. 13 - Prob. 20RECh. 13 - Prob. 21RECh. 13 - Prob. 22RECh. 13 - Prob. 23RECh. 13 - REFLECT AND APPLY What are the requirements for an...Ch. 13 - Prob. 25RECh. 13 - Prob. 26RECh. 13 - REFLECT AND APPLY The genes for both the a- and...Ch. 13 - REFLECT AND APPLY Outline the methods you would...Ch. 13 - Prob. 29RECh. 13 - Prob. 30RECh. 13 - Prob. 31RECh. 13 - Prob. 32RECh. 13 - RECALL Why is temperature control so important in...Ch. 13 - RECALL Why is the use of temperature-stable DNA...Ch. 13 - RECALL What are the criteria for good primers in a...Ch. 13 - REFLECT AND APPLY What difficulties arise in the...Ch. 13 - REFLECT AND APPLY Each of the following pairs of...Ch. 13 - RECALL What is qPCR?Ch. 13 - Prob. 39RECh. 13 - REFLECT AND APPLY Suppose that you are a...Ch. 13 - REFLECT AND APPLY Why is DNA evidence more useful...Ch. 13 - REFLECT AND APPLY Give the DNA sequence for the...Ch. 13 - Prob. 43RECh. 13 - Prob. 44RECh. 13 - Prob. 45RECh. 13 - Prob. 46RECh. 13 - Prob. 47RECh. 13 - RECALL Has proteomic analysis been done on...Ch. 13 - Prob. 49RECh. 13 - Prob. 50RECh. 13 - Prob. 51RECh. 13 - RECALL What are the key differences between DNA...
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- 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 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_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_forward
- 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. 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_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_forward
- The 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_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_forward
- Which 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_forward
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