QUESTION 27If you mixed SDS with the protein below and ran it in SDS-PAGE, how many bands would you expect to appear on the gel after coomassie staining?-s-s-O 1O 2O 4O too many to count

SDS-PAGE or Sodium Dodecylsulphate- Poly Acrylamide Gel Electrophoresis is a molecular technique to…

Answered: QUESTION 27 If you mixed SDS with the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Question for protein crystallography- 1. While performing a routine protein crystallization screening, you observe that one of your well drops has doubled in size compared to the remaining wells. Note: the drop in question was set up by taking 1 µL of the protein solution (10 mg/mL LDH in 20 mM TRIS pH 7.5, 0.5 M NaCl and 10% PEG 4000K) and adding it to 1 µL of the crystallization solution (10% PEG 4000K, 50 mM NaCl and 20 mM TRIS pH 8.0). Why did this drop grow larger in size compared to when you initially set it up?
Question 4
QUESTION 22 Which of the following types of interactions are not made between R groups of proteins? Hydrogen bonds lonic bonds Disulfide bridges or disulfide bonds O All of the above are found between R groups QUESTION 23 Which of the following is not true regarding DNA? Complementary DNA strands are anti-parallel to one another DNA is usually double stranded DNA utilizes thymine DNA nucleotides include ribose
Question 1 In DNA, with which base does guanine pair? O another guanine O cytosine O thymine O adenine
QUESTION 17 A student wanted to run a protein sample on a SDS PAGE gel, and in the process of casting a gel the student had forgotten to add the stacking layer on top of the resolving layer of the gel. What problems would likely arise as a result of this mishap? Proteins would migrate much faster through the gel Proteins would not be able to migrate through the resolving layer and stays at the top of the gel Proteins will move into the resolving layer at different times and this would result in a smear on the gel There is no problem, proteins in the sample would resolve the same as if they were ran on a SDS PAGE gel with a stacking layer on top of a resolving layer QUESTION 18 Sample A is diluted by adding 50 ul to 950 uL of buffer to make solution B. Solution B is diluted by adding 50 uL of solution B to 300 uL of buffer. The absorbance of sample C is 0.05. What is the concentration of sample A assuming the following parameters. |=1 cm Molar extinction coefficient = 10 M-1 cm-1 O 0.7…
QUESTION 6 If the 3 proteins in the blue sample had MW's of [1] 87,000 Daltons, [2] 30,000 Daltons, [3] 15,000 Daltons; what is the MW of the protein in the 2nd band (counting from the origin) of the green sample? O O O O a. about 15,000 daltons b. about 87,000 daltons c. more than 30,000 daltons but less than 87,000 daltons d. about 30,000 daltons Cellular and Molecular Biology (6657
Question 10 Produce the complimentary DNA strand that would be matched with the provided strand T--A C-- G C-- G A -- A -- C-- G-- T-- T-- A -- C-- G -- G--
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Question 12
Question 1 Listen If you are given a sample with 1,000,000 pfu/mL of bacteriophage (Tube A) and plate 1mL of the sample on a TSA plate, what will you observe after 24 hours incubation? (How many plaques?) 100,000 because it is a 1:10 dilution. Zero because bacteriophage need a host to grow. More than 300 because it will be TNTC. 1,000,000 plaques because there are 1,000,000 phage in 1mL.
Question 7 of 10 Question 7. You are studying two strands of DNA. They have exactly the same length, but the first one has a very high G + C/A +T ratio of 3.4. The second DNA strand has a G + C/A + T ratio of 2.3. Which of the two strands will have the lowest melting temperature and why?
40

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QUESTION 27 If you mixed SDS with the protein below and ran it in SDS-PAGE, how many bands would you expect to appear on the gel after coomassie staining? -s-s- O 1 O2 O 4 O too many to count