Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 4, Problem 3RE
RECALL What is the nature of “random” structure in proteins?
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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 4 Solutions
Biochemistry
Ch. 4 - RECALL Match the following statements about...Ch. 4 - RECALL Define denaturation in terms of the effects...Ch. 4 - RECALL What is the nature of random structure in...Ch. 4 - REFLECT AND APPLY Suggest an explanation for the...Ch. 4 - REFLECT AND APPLY Rationalize the following...Ch. 4 - REFLECT AND APPLY Glycine is a highly conserved...Ch. 4 - REFLECT AND APPLY A mutation that changes an...Ch. 4 - REFLECT AND APPLY A biochemistry student...Ch. 4 - RECALL List three major differences between...Ch. 4 - RECALL What are Ramachandran angles?
Ch. 4 - Prob. 11RECh. 4 - Prob. 12RECh. 4 - RECALL List some of the differences between the...Ch. 4 - RECALL List some of the possible combinations of...Ch. 4 - RECALL Why is proline frequently encountered at...Ch. 4 - RECALL Why must glycine be found at regular...Ch. 4 - REFLECT AND APPLY You hear the comment that the...Ch. 4 - REFLECT AND APPLY Woolen clothing shrinks when...Ch. 4 - RECALL Draw two hydrogen bonds, one that is part...Ch. 4 - RECALL Draw a possible electrostatic interaction...Ch. 4 - RECALL Draw a disulfide bridge between two...Ch. 4 - RECALL Draw a region of a polypeptide chain...Ch. 4 - REFLECT AND APPLY The terms configuration and...Ch. 4 - REFLECT AND APPLY Theoretically, a protein could...Ch. 4 - REFLECT AND APPLY What is the highest level of...Ch. 4 - RECALL List two similarities and two differences...Ch. 4 - RECALL What are the two critical amino acids near...Ch. 4 - RECALL What is the highest level of organization...Ch. 4 - RECALL Suggest a way in which the difference...Ch. 4 - RECALL Describe the Bohr effect.Ch. 4 - RECALL Describe the effect of 2,...Ch. 4 - RECALL How does the oxygen-binding curve of fetal...Ch. 4 - RECALL What is the critical amino acid difference...Ch. 4 - REFLECT AND APPLY In oxygenated hemoglobin,...Ch. 4 - REFLECT AND APPLY You are studying with a friend...Ch. 4 - REFLECT AND APPLY How does the difference between...Ch. 4 - REFLECT AND APPLY Suggest a reason for the...Ch. 4 - Prob. 38RECh. 4 - REFLECT AND APPLY Why is fetal Hb essential for...Ch. 4 - BIOCHEMICAL CONNECTIONS Why might you expect to...Ch. 4 - REFLECT AND APPLY When deoxyhemoglobin was first...Ch. 4 - BIOCHEMICAL CONNECTIONS What is the direct cause...Ch. 4 - BIOCHEMICAL CONNECTIONS What is the effect of the...Ch. 4 - BIOCHEMICAL CONNECTIONS Why do scientists believe...Ch. 4 - Prob. 45RECh. 4 - BIOCHEMICAL CONNECTIONS What is BCL11A and how is...Ch. 4 - BIOCHEMICAL CONNECTIONS Given the purpose of...Ch. 4 - Prob. 48RECh. 4 - REFLECT AND APPLY Comment on the energetics of...Ch. 4 - RECALL What is a chaperone?Ch. 4 - Prob. 52RECh. 4 - Prob. 53RECh. 4 - Prob. 54RECh. 4 - RECALL What are some diseases caused by misfolded...Ch. 4 - RECALL What causes protein aggregates to form?Ch. 4 - Prob. 57RECh. 4 - Prob. 58RECh. 4 - BIOCHEMICAL CONNECTIONS What aspects of the...Ch. 4 - Prob. 60RECh. 4 - Prob. 61RE
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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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