EBK BIOCHEMISTRY
6th Edition
ISBN: 9781337431200
Author: GRISHAM
Publisher: CENGAGE LEARNING - CONSIGNMENT
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Textbook Question
Chapter 29, Problem 4P
Comparison of Prokaryotic and Eukaryotic Transcription Make a list of the ways that transcription in eukaryotes differs from transcription in prokaryotes.
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The rate data from an enzyme catalyzed reaction with and without an inhibitor present is found in the image.
Question: what is the KM and Vm and the nature of inhibition
1. Estimate the concentration of an enzyme within a living cell. Assume that:
(a): fresh tissue is 80% water and all of it is intracellular
(b): the total soluble protein represents 15% of the weight
(c): all the soluble proteins are enzymes
(d): the average molecular weight of the proteins is 150,000
(E): about 100 different enzymes are present
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Chapter 29 Solutions
EBK BIOCHEMISTRY
Ch. 29 - Prob. 1PCh. 29 - The Events in Transcription Initiation Describe...Ch. 29 - Substrate Binding by RNA Polymerase RNA polymerase...Ch. 29 - Comparison of Prokaryotic and Eukaryotic...Ch. 29 - Prob. 5PCh. 29 - Prob. 6PCh. 29 - Prob. 7PCh. 29 - Alternative Splicing Possibilities Suppose exon 17...Ch. 29 - Prob. 9PCh. 29 - Prob. 10P
Ch. 29 - Post-transcriptional Modification of Eukaryotic...Ch. 29 - Prob. 12PCh. 29 - Prob. 13PCh. 29 - The Lariat Intermediate in RNA Splicing Draw the...Ch. 29 - Prob. 15PCh. 29 - Prob. 16PCh. 29 - Prob. 17PCh. 29 - Prob. 18PCh. 29 - Figure 29.15 highlights in red the DNA phosphate...Ch. 29 - Chromatin decompaction is a preliminary step in...
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- The following data were recorded for the enzyme catalyzed conversion of S -> P. Question: Estimate the Vmax and Km. What would be the rate at 2.5 and 5.0 x 10-5 M [S] ?arrow_forwardPlease helparrow_forwardThe following data were recorded for the enzyme catalyzed conversion of S -> P Question: what would the rate be at 5.0 x 10-5 M [S] and the enzyme concentration was doubled? Also, the rate given in the table is from product accumulation after 10 minuets of reaction time. Verify these rates represent a true initial rate (less than 5% turnover). Please helparrow_forward
- The following data was obtained on isocitrate lyase from an algal species. Identify the reaction catalyzed by this enzyme, deduce the KM and Vmax , and determine the nature of the inhibition by oxaloacetate. Please helparrow_forwardIn the table below, there are sketches of four crystals made of positively-charged cations and negatively-charged anions. Rank these crystals in decreasing order of stability (or equivalently increasing order of energy). That is, select "1" below the most stable (lowest energy) crystal. Select "2" below the next most stable (next lowest energy) crystal, and so forth. A B 鹽 (Choose one) +2 C +2 +2 (Choose one) D 鹽雞 (Choose one) (Choose one)arrow_forward1. Draw the structures for the fats A. 16:2: w-3 and B. 18:3:49,12,15 2. Name each of the molecules below (image attached)arrow_forward
- draw the structures for the fats A. 16:2:w-3 B 18:3:9,12,15arrow_forward1. Below is a template strand of DNA. Show the mRNA and protein that would result. label the ends of the molecules ( refer to attached image)arrow_forwardAttach the followina labels to the diagram below: helicase, single stranded binding proteins, lagging strand, leading strand, DNA polymerase, primase, 5' ends (3), 3' ends (3) (image attached)arrow_forward
- 1. How much energy in terms of ATP can be obtained from tristearin (stearate is 18:0) Show steps pleasearrow_forwardMultiple choice urgent!!arrow_forward1. Write the transamination reaction for alanine. Indicate what happens next to each of the molecules in the reaction, and under what conditions it happens. 2.arrow_forward
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