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 61RE
Interpretation Introduction
Interpretation:
The ways in which the facts are related to the transmission of prion disease is to be explained.
Concept Introduction:
Prions are misfolded proteins which characterize several fatal neurodegenerative diseases in animal and humans.
The normal and abnormal prions differ in the protein structure.
They are even smaller than viruses and do not have
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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!
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 help
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?
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. 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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