Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 3, Problem 24RE
RECALL Sketch resonance structures for the peptide group.
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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
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Chapter 3 Solutions
Biochemistry
Ch. 3 - RECALL How do D-amino acids differ from L-amino...Ch. 3 - RECALL Which amino acid is technically not an...Ch. 3 - RECALL For each of the following, name an amino...Ch. 3 - RECALL Identify the polar amino acids, the...Ch. 3 - RECALL Identify the nonpolar amino acids and the...Ch. 3 - RECALL Are amino acids other than the usual 20...Ch. 3 - MATHEMATICAL Predict the predominant ionized forms...Ch. 3 - MATHEMATICAL Draw structures of the following...Ch. 3 - MATHEMATICAL Predict the predominant forms of the...Ch. 3 - MATHEMATICAL Calculate the isoelectric point of...
Ch. 3 - MATHEMATICAL Sketch a titration curve for the...Ch. 3 - MATHEMATICAL Sketch a titration curve for the...Ch. 3 - MATHEMATICAL An organic chemist is generally happy...Ch. 3 - MATHEMATICAL Sketch a titration curve for aspartic...Ch. 3 - REFECT AND APPLY Suggest a reason why amino acids...Ch. 3 - REFECT AND APPLY Write equations to show the ionic...Ch. 3 - REFECT AND APPLY Based on the information in Table...Ch. 3 - REFECT AND APPLY If you were to have a mythical...Ch. 3 - REFECT AND APPLY What would be the pI for the...Ch. 3 - REFECT AND APPLY Identify the charged groups in...Ch. 3 - REFECT AND APPLY Consider the following peptides:...Ch. 3 - REFECT AND APPLY In each of the following two...Ch. 3 - REFECT AND APPLY Could the amino acid glycine...Ch. 3 - RECALL Sketch resonance structures for the peptide...Ch. 3 - RECALL How do the resonance structures of the...Ch. 3 - REFECT AND APPLY Would the peptide group be planar...Ch. 3 - Prob. 27RECh. 3 - REFECT AND APPLY Consider the peptides...Ch. 3 - REFECT AND APPLY Would you expect the titration...Ch. 3 - REFECT AND APPLY What are the sequences of all the...Ch. 3 - REFECT AND APPLY Answer Question 30 using...Ch. 3 - REFECT AND APPLY Most proteins contain more than...Ch. 3 - REFECT AND APPLY If the amino acids alanine and...Ch. 3 - Prob. 34RECh. 3 - REFECT AND APPLY Would the presence of a chiral...Ch. 3 - REFECT AND APPLY What might you infer (or know)...Ch. 3 - Prob. 37RECh. 3 - REFECT AND APPLY Suggest a reason why the amino...Ch. 3 - REFECT AND APPLY Consider the peptides...Ch. 3 - Prob. 40RECh. 3 - Prob. 41RECh. 3 - REFECT AND APPLY You are studying with a friend...Ch. 3 - Prob. 43RECh. 3 - REFECT AND APPLY Suggest a reason (or reasons) why...Ch. 3 - Prob. 45RECh. 3 - REFECT AND APPLY Speculate on the properties of...Ch. 3 - RECALL What are the structural differences between...Ch. 3 - RECALL How do the peptide hormones oxytocin and...Ch. 3 - RECALL What is the role of the disulfide bond in...Ch. 3 - RECALL Is it possible to form cyclic peptides...Ch. 3 - Prob. 51RECh. 3 - RECALL What types of experiments led to evidence...Ch. 3 - Prob. 53RECh. 3 - THOUGHT QUESTION Imagine we identify a gene that...
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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.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
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