Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 31, Problem 17P
Interpretation Introduction
Interpretation:
Number of bands of 70S ribosomes formed in the centrifugal tube should be determined.
Concept introduction:
The complex composition of rRNA (ribosomal RNA) and protein molecules are termed as ribosomes. It acts as a factory for the process of protein synthesis. They are mostly found attached to endoplasmic reticulum, and some ribosomes are found to suspend freely in the cytoplasm of the cell.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
.A protein gives a single band on SDS gel electrophoresis, as shown
in lanes 1 and 2 below. There is little if any effect from adding
proteins. Which of the following will tell you whether a protein would be found in the lumen of the ER?
A. You run a hydropathy plot an look for hydrophobic peaks that span 20-30 amino acids
B. You isolate microsomes and see whether the proteins are inserted into the membrane of the microsome
C. You run a hydropathy plot an look for a lack of hydrophobic peaks that span 20-30 amino acids
O D. You do in vitro translation of each protein in the presence or absence of microsomes and look to see whether there is a size change in the presence
of microsomes.
In Multi-Column Purification of rGFP.
What happens to the protein amount, protein purity, and/or specific activity of a purification fraction if one of the three is changed? (i.e. understand the relationship between the three.)
Chapter 31 Solutions
Biochemistry
Ch. 31 - Prob. 1PCh. 31 - Prob. 2PCh. 31 - Prob. 3PCh. 31 - Prob. 4PCh. 31 - Prob. 5PCh. 31 - Prob. 6PCh. 31 - Prob. 7PCh. 31 - Prob. 8PCh. 31 - Prob. 9PCh. 31 - Prob. 10P
Ch. 31 - Prob. 11PCh. 31 - Prob. 12PCh. 31 - Prob. 13PCh. 31 - Prob. 14PCh. 31 - Prob. 15PCh. 31 - Prob. 16PCh. 31 - Prob. 17PCh. 31 - Prob. 18PCh. 31 - Prob. 19PCh. 31 - Prob. 20PCh. 31 - Prob. 21PCh. 31 - Prob. 22PCh. 31 - Prob. 23PCh. 31 - Prob. 24PCh. 31 - Prob. 25PCh. 31 - Prob. 26PCh. 31 - Prob. 27PCh. 31 - Prob. 28PCh. 31 - Prob. 29PCh. 31 - Prob. 30PCh. 31 - Prob. 31PCh. 31 - Prob. 32PCh. 31 - Prob. 33PCh. 31 - Prob. 34PCh. 31 - Prob. 35PCh. 31 - Prob. 36PCh. 31 - Prob. 37PCh. 31 - Prob. 38PCh. 31 - Prob. 39PCh. 31 - Prob. 40PCh. 31 - Prob. 41PCh. 31 - Prob. 42PCh. 31 - Prob. 43PCh. 31 - Prob. 44PCh. 31 - Prob. 45PCh. 31 - Prob. 46PCh. 31 - Prob. 47PCh. 31 - Prob. 48PCh. 31 - Prob. 49PCh. 31 - Prob. 50PCh. 31 - Prob. 51PCh. 31 - Prob. 52P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Please help me with this question. How many amino acid residues are in the heavy and light chains of the Fab fragment, and how many amino acid residues are in lysozyme?arrow_forwardPurification of a new unknown protein that you isolated from tissue and Assume that you have reached the following data during the characterization; Gel filtration: Gel filtration in protein native conformation When chromatographed, it has a molecular weight of 240000 daltons (240 kDa) is detected to be around. Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride subjected to gel filtration chromatography again under denatured conditions. is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa) a protein is obtained. SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol (Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons. Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa) is observed. In the light of these findings, the quaternary/quaternary…arrow_forwardMovement of Dyes in an Agarose Gel.This problem tests your ability to understand basic concepts of agarose gel electrophoresis.The gel is loaded from lane 1 at the top to lane 7 at the bottom with: bromophenol blue, safranin O, orange G, crystal violet, xylene cyanol, methylene blue, and the unknown.Lines have been added to the gel to help you locate the center of the wells. Which known dye samples are positively charged? Which known dyes are in the unknown sample in lane 7?arrow_forward
- Affinity chromatography You have created a fusion protein tagged with Glutathione-S-Transferase (GST). Your lab mate tells you that the affinity columns for this type of tagged protein are very similar to that of Histadine tagged proteins. Using the following elements set up a purification column and construct a protocol for an affinity purification using this tag. A large amount of glutathione is usually used to elute the tagged protein off the column. How might this work?arrow_forward. Explain why DNA is stable in the presence of alkali (0.3 M KOH), while RNA is quantitatively degraded to 2'- and 3'-nucleoside monophosphates under these conditions.arrow_forwardAnabolism & Catabolism of Nitrogenous Bases. a. Differentiate the processes of purine nucleotide biosynthesis & pyrimidine nucleotide biosynthesis. What are the starting materials for each process? b. Differentiate the processes of purine nucleotide degradation &pyrimidine nucleotide degradation. What are the end products of each process? c. Explain how purine & pyrimidine biosynthesis is regulated to produce balanced levels ofall four nucleotides (ATP, GTP, UTP & CTP)?arrow_forward
- disadvantage of using protein blastarrow_forwardUsing Fig. as a guide, draw the complete structure of a nucleoside triphosphate before and after it becomes incorporated into a polynucleotide chain. Draw the structure that would result if the newly formed phosphodiester bond were hydrolyzed.arrow_forwardHurray! The bacteria did their job and expressed your protein. Now, you need to isolate biochemisfunase from the other bacterial proteins. To do this, you first need to break open the bacterial cells, a process called cell lysis. The lysis buffer you are going to use requires 225 mM potassium chloride (KCl), which is available as a crystalline solid. The lysis buffer also requires 22.5% (v/v) glycerol, which is available as a 100% stock solution. Describe how you would make 250 ml of lysis buffer and show all calculations.arrow_forward
- Why is ti advantageous for a cell to expend metabolic energy to polymerize gulucose molecule.?arrow_forwardHurray! The bacteria did their job and expressed your protein. Now, you need to isolate biochemisfunase from the other bacterial proteins. To do this, you first need to break open the bacterial cells, a process called cell lysis. The lysis buffer you are going to use requires 225 mM potassium chloride (KCl), which is available as a crystalline solid. The lysis buffer also requires 22.5% (v/v) glycerol, which is available as a 100% stock solution. When making your lysis buffer,you added too much water,and you ended up with 375 ml of lysis buffer solution. The postdoc you are working with, underpaid and overworked, tells you to “rescue” the solution rather than remaking it. This same postdoc tells you that concentration is more important than the final volume. How would you go about rescuing the solution? (To make the required lysis buffer, take 56.25 mL of the 100% glycerol stock and add 193.75 mL water to it.)arrow_forwardTrue or false .Very powerful X-rays used in crystallography are generated in a very large facilities called synchrotron .A western blot allows detection of proteins after SDS-PAGE with higher sensitivit .Keratin and collagen adopt helical structures whereas silk fibroin adopts beta sheet structures .arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY 
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY