Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 6, Problem 14P
A protein gives a single band on SDS get electrophoresis, as shown in lanes 1 and 2 below. There is little, if any, effect from adding
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 inlanes 1 and 2 below. There is little, if any, effect from adding β-mercaptoethanol (BME) to the sample; if anything, the protein runs a little bitslower. When treated with the proteolytic enzyme thrombin and electrophoresis in the absence of BME, the protein migrates a bitmore rapidly (lane 3). But if BME is present, two much more rapidlymigrating bands are found (lane 4). Explain these results in terms of amodel for the protein.
A good way to increase total proteome coverage without using 2D PAGE is to:
"Use two, orthogonal types of chromatography"
Enrich for phosphopeptides only
Analyze whole proteins instead of proteolytic peptides.
Calculate these for 1 ug of plasmid DNA in a final total volume of 20 ul. All
enzymes being used here are at a concentration of 10 U/µL. For double digests, give the
appropriate volume for each enzyme and decide which buffer to use. (HINT: look up double
digest conditions on the NEB website.) You should always calculate all volumes in advance to
ensure the correct working concentrations and so that you can prepare the digests as efficiently
as possible. It is a good idea to check off each component as it is added to the microfuge tube.
Complete the table below, including the volume of DNA sample(s) you will need for 1 pg of the
DNA (from two different methods in Experiment #3) based on the concentration(s) you
determined from the OD260 value, which you will restriction digest with each of the restriction
enzymes singly and in double digests in Part A.
For example, the volume of DNA sample that contains 1 µg DNA for DNA sample from Part A,
Experiment 3: OD260 = 0.024, dilution 500x…
Chapter 6 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 6 - Prob. 1PCh. 6 - Bovine pancreatic trypsin inhibitor (BPTI; Figure...Ch. 6 - A schematic structure of the subunit of...Ch. 6 - In the protein adenylate kinase, the C-terminal...Ch. 6 - Give two reasons to explain why a proline residue...Ch. 6 - Consider a small protein containing 101 amino acid...Ch. 6 - a. Based on a more conservative answer to Problem...Ch. 6 - The following sequence is part of a globular...Ch. 6 - a. A protein is found to be a tetramer of...Ch. 6 - Under physiological conditions, the protein...
Ch. 6 - Theoretical and experimental measurements show...Ch. 6 - The peptide hormone vasopressin is used in the...Ch. 6 - A protein gives under conditions of buffer...Ch. 6 - A protein gives a single band on SDS get...Ch. 6 - It has been postulated that the normal...Ch. 6 - Below are shown two views of the backbone...Ch. 6 - Do you expect a Pro Gly mutation in a...Ch. 6 - Rank the following in terms of predicted rates...Ch. 6 - Shown below are two cartoon views of the small...Ch. 6 - Prob. 20PCh. 6 - In most cases, mutations in the core of protein...Ch. 6 - A Leu Ala mutation at a site buried the core of...Ch. 6 - Disulfide bonds have been shown to stabilize...Ch. 6 - Cartoon renderings of the proteins Top 7 and adaH2...
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
- in isolating ribosomes from a yield sample, describe the ideal type of centrifugation for this separation technique based on the following:*Type of Centrifugation* Type of fraction *Give 2 advantages of using this type of centrifuge.*Give 2 disadvantages of using this type of centrifuge.arrow_forwardElectrophoretic Analysis of DNA via Agarose gel Electrophoresis determine the voltage used (how to determine the voltage? Hint: check on volt/cm).arrow_forwardIn an in vitro motility assay, a newly discovered motor protein is found to transport an attached bead along a microtubule away from the end where fluorescent labeled tubulin dimers assembled. Which of the following are true? Select all that apply The motor protein is transporting the bead towards the minus end The motor protein is transporting the bead towards the plus end The motor protein belongs to the dynein family The motor protein belongs to the kinesin family Oarrow_forward
- Transferring of the protein bands from the SDS-PAGE gel to the PDVF membrane can be troublesome and sometimes incomplete. What are some reasons (at least 3) why the transfer step wouldn’t work?arrow_forwardIn your own words, describe how we will use hydrophobic interaction chromatography to purify GFP from the multitude of other proteins in a bacterial cell. Be sure to include the purpose of each of the wash solutions in the process (Equilibration, Binding, Wash, and Elution Buffers).arrow_forwardGiven this, if you used 6g of vitamin Z powder to make 20 ml of solution, what is the % concentration of this solution? (I gave the image since I don't know if that info is needed to solve this question.)It also gives a follow-up, if you can help here too: You work in a lab as a summer student. One of your tasks is to make sure that there is enough cell culture medium containing antibiotics to grow bacteria. One day you realize that there is only 5 ml of 10% Antibiotic stock solution in the freezer. You decide to use it all to prepare the working culture medium with 0.01% antibiotic. In the lab there is plenty of growth medium without antibiotics. (Note: dilution in medium is like dilution in water). You remember the equation to make dilutions of stock solutions. You usually use this formula to calculate the required volume of a stock solution, but you realize it can apply here as well, even though the unknown is the final volume. So, you make that dilution. Given that each bacterial…arrow_forward
- Protein analysis by gel electrophoresis a). Using the gel image provided to calculate the electrophoretic relative mobility as a ratio of the distance of protein migration to the distance of the tracking dye migration (See Appendix B). If your dye front is not visible, measure the mobility relative to the bottom edge of the resolving gel. Include a labeled print-out of your gel image with your report. b). Plot log MW of the protein markers and commercial myoglobin vs. mobility. Determine the molecular weight of myoglobin obtained after the final purification step (Sample E) from the equation of the line. Submit a copy of your graph along with the gel image. c). Compare your sample E and commercial myoglobin with the ladder. Summary your results. order of sample (left to right) is : A B C D blank E blank Commercial Myoglobin Molecular Ladderarrow_forwardHIC chromatography does not yield 100% pure GFP. What other types of cellular proteins would most likely be found in the GFP preparation?arrow_forwardCan you please help me to make a professional table with excel I don’t know how to use exell thanks youarrow_forward
- Using a schematic diagram, summarize the following steps in preparing competent cells for transformation: Inoculate a single colony of E. coli into 5 ml LB broth and incubate overnight at 37°C with moderate shaking (250 rpm). Add 200 μl of the culture into 50 ml LB broth and incubate overnight at 37°C with moderate shaking (250 rpm) to an OD600 = 1.3 to 1.5. Aliquot culture into five 15-ml pre-chilled, conical tubes. Leave tube on ice 5 to 10 min. Centrifuge cells 7 min at 1,600 × g (3,000 rpm), 4°C. Pour off supernatant and resuspend each pellet in 10 ml ice-cold CaCl2 solution (50 mM CaCl2), perform resuspension very gently, and keep on ice. Centrifuge cells 5 min at 1,100 × g (2,500 rpm), 4°C. Discard supernatant and resuspend each pellet in 10 ml ice-cold CaCl2 solution. Keep resuspended on ice for 30 min. Centrifuge cells 5 min at 1,100 × g, 4°C. Discard supernatant and resuspend each pellet in 10 ml ice-cold CaCl2 solution. Dispense cells (250 μl) into pre-chilled, sterile…arrow_forwardIn size exclusion chromatography, which component will elute last in the set up? O Small proteins will elute last because they do not pass through the pores of the gel beads. O Large proteins will elute last because they pass through the pores of the gel beads. O Small proteins will elute last because they pass through the pores of the gel beads. Large proteins will elute last because they do not pass through the pores of the gel beads.arrow_forwardThe table below shows the response of our ESKAPE safe relatives to 4 bacteria isolated from a master grid. We do not know the identity or any characteristics of the unknown bacteria. Each safe relative was spread onto a petri dish using aseptic technique. A grid pattern was taped to each plate and the unknown bacteria were patched into one of the squares. If there was no inhibition visible, including with a magnifying lens, the result was listed as -. If there was an inhibition zone between 1 and 10mm in diameter, the result is listed as +. If the inhibition zone was 10mm or greater, the result is listed as ++. In the lab, the MGC instructors plated all 6 of the ESKAPE pathogen safe relatives on LB agar plates. Then we patched Unknown Bacteria 5 from a Master plate onto the safe relative. The results are shown here: METRIC METRIC METRIC 1 B. subtilis S. epidermidis E. coli Complete the final column (Unknown Bacteria 5) of the table by selecting -, +, or ++ using the criteria in the…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