Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 22, Problem 21RE
Interpretation Introduction
Interpretation:
The source of oxygen is to be identified, out of water and carbon dioxide, and the reason for the same is to be explained.
Concept Introduction:
The
During the light reaction, the reduction of
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Students have asked these similar questions
Complete the sentences describing membrane lipids by moving the names of the lipids to the appropriate sentence. Some lipids
will be used more than once, and some sentences will require you to place two or three lipids.
Answer Bank
include two fatty acids joined to glycerol by ester linkages.
do not contain glycerol.
is a steroid.
contain a sphingosine backbone.
contain one or more sugars.
usually have branched alkyl chains.
glycolipids
phosphoglycerides
sphingomyelin
cholesterol
archacal lipids
The protein content of most plasma membranes is, on average, about 50% by weight. Myelin has a protein content of about 18%,
whereas the internal membranes of mitochondria and chloroplasts may be composed of 75% protein.
Label the membrane proteins on the diagram.
Answer Bank
lipid-anchored protein
peripheral membrane protein
integral membrane protein
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)?
Chapter 22 Solutions
Biochemistry
Ch. 22 - Prob. 1RECh. 22 - RECALL The bean sprouts available at the grocery...Ch. 22 - Prob. 3RECh. 22 - RECALL How is the structure of chloroplasts...Ch. 22 - Prob. 5RECh. 22 - Prob. 6RECh. 22 - Prob. 7RECh. 22 - Prob. 8RECh. 22 - Prob. 9RECh. 22 - Prob. 10RE
Ch. 22 - Prob. 11RECh. 22 - Prob. 12RECh. 22 - Prob. 13RECh. 22 - Prob. 14RECh. 22 - Prob. 15RECh. 22 - REFLECT AND APPLY Albert Szent-Gyorgi, a pioneer...Ch. 22 - Prob. 17RECh. 22 - Prob. 18RECh. 22 - Prob. 19RECh. 22 - Prob. 20RECh. 22 - Prob. 21RECh. 22 - Prob. 22RECh. 22 - Prob. 23RECh. 22 - Prob. 24RECh. 22 - Prob. 25RECh. 22 - Prob. 26RECh. 22 - RECALL In cyclic photophosphorylation in...Ch. 22 - Prob. 28RECh. 22 - Prob. 29RECh. 22 - Prob. 30RECh. 22 - Prob. 31RECh. 22 - Prob. 32RECh. 22 - Prob. 33RECh. 22 - Prob. 34RECh. 22 - Prob. 35RECh. 22 - Prob. 36RECh. 22 - Prob. 37RECh. 22 - REFLECT AND APPLY If photosynthesizing plants are...Ch. 22 - Prob. 39RECh. 22 - Prob. 40RECh. 22 - Prob. 41RECh. 22 - Prob. 42RECh. 22 - Prob. 43RECh. 22 - Prob. 44RECh. 22 - Prob. 45RECh. 22 - Prob. 46RECh. 22 - RECALL How does photosynthesis in C4 plants differ...Ch. 22 - Prob. 48RECh. 22 - Prob. 49RECh. 22 - Prob. 50RE
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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: LDHarrow_forwardPlease helparrow_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. Describe the architecture of the polypeptide component of this enzyme.arrow_forward
- 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
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