Owlv2,1 Term Printed Access Card For Campbell/farrell/mcdougal's Biochemistry, 9th
9th Edition
ISBN: 9781305962972
Author: Campbell, Mary K.; Farrell, Shawn O.; Mcdougal, Owen M.
Publisher: Cengage Learning
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Chapter 1, Problem 20RE
RECALL Draw an idealized plant cell, and identify the parts by name and function.
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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?
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Chapter 1 Solutions
Owlv2,1 Term Printed Access Card For Campbell/farrell/mcdougal's Biochemistry, 9th
Ch. 1 - RECALL State why the following terms are important...Ch. 1 - RECALL Match each entry in Column a with one in...Ch. 1 - RECALL Identify the functional groups in the...Ch. 1 - REFLECT AND APPLY In 1828, Wohler was the first...Ch. 1 - REFLECT AND APPLY A friend who is enthusiastic...Ch. 1 - REFLECT AND APPLY Does biochemistry differ from...Ch. 1 - REFLECT AND APPLY An earlier mission to Mars...Ch. 1 - REFLECT AND APPLY Common proteins are polymers of...Ch. 1 - REFLECT AND APPLY Nucleic acids are polymers of...Ch. 1 - REFLECT AND APPLY RNA is often characterized as...
Ch. 1 - REFLECT AND APPLY Why is the development of...Ch. 1 - REFLECT AND APPLY What are two major advantages of...Ch. 1 - REFLECT AND APPLY Why was the development of a...Ch. 1 - REFLECT AND APPLY Comment on RNAs role in...Ch. 1 - REFLECT AND APPLY Do you consider it a reasonable...Ch. 1 - RECALL List five differences between prokaryotes...Ch. 1 - RECALL Do the sites of protein synthesis differ in...Ch. 1 - REFLECT AND APPLY Assume that a scientist claims...Ch. 1 - RECALL Draw an idealized animal cell, and identify...Ch. 1 - RECALL Draw an idealized plant cell, and identify...Ch. 1 - RECALL What are the differences between the...Ch. 1 - RECALL Which organelles are surrounded by a double...Ch. 1 - RECALL Which organelles contain DNA?Ch. 1 - RECALL Which organelles are the sites of...Ch. 1 - RECALL State how the following organelles differ...Ch. 1 - RECALL List the five kingdoms into which living...Ch. 1 - RECALL Which of the five kingdoms consist of...Ch. 1 - RECALL How does the five-kingdom classification...Ch. 1 - REFLECT AND APPLY What are the advantages of being...Ch. 1 - REFLECT AND APPLY Mitochondria and chloroplasts...Ch. 1 - REFLECT AND APPLY Fossil evidence indicates that...Ch. 1 - RECALL Which processes are favored: those that...Ch. 1 - RECALL Does the thermodynamic term spontaneous...Ch. 1 - BIOCHEMICAL CONNECTIONS For the process...Ch. 1 - RECALL Which of the following are spontaneous...Ch. 1 - REFLECT AND APPLY In which of the following...Ch. 1 - REFLECT AND APPLY Why is it necessary to specify...Ch. 1 - REFLECT AND APPLY Why is the entropy of a system...Ch. 1 - REFLECT AND APPLY A reaction at 23C has G=1kJmol1....Ch. 1 - REFLECT AND APPLY Urea dissolves very readily in...Ch. 1 - REFLECT AND APPLY Would you expect the reaction...Ch. 1 - REFLECT AND APPLY The existence of organelles in...Ch. 1 - REFLECT AND APPLY Why is it advantageous for a...Ch. 1 - REFLECT AND APPLY Which would you expect to have a...Ch. 1 - REFLECT AND APPLY How would you modify your answer...Ch. 1 - REFLECT AND APPLY Would it be more or less likely...Ch. 1 - REFLECT AND APPLY What thermodynamic...Ch. 1 - REFLECT AND APPLY If cells of the kind we know...Ch. 1 - REFLECT AND APPLY The process of protein folding...Ch. 1 - REFLECT AND APPLY In biochemistry, the exergonic...
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- 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
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