Thanks in advance!Homework Answers
1)-size-exclusion chromatography separate protein according to their size.
2)-isoelectric focusing used for separating different molecules by difference in their isoelectric point.
3)-two dimensional electrophoresis because it is used to analyze protein.
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Thanks in advance! 1.33/2 pts Partial Question 2 1. Which of these protein separation methods would be the most useful f...
Can someone answer the question and provide a short explanation? Thanks! Which of the following statements...
Can someone answer the question and provide a short explanation? Thanks! Which of the following statements is NOT correct regarding protein seperation techniques? A) Size-exclusion chromatography works on the same principle as polyacrylamide gel electrophoresis B) Specific antibodies are required for immunoblotting, antibody affinity chromatography as well as immunoprecipitation C) Two-dimensional gel electrophoresis is conceptually the same as combining gel filtration chromatography and ion exchange chromatography D) Western blotting is a useful technique to isolate proteins for use in downstream...
Can someone help me answers these? These questions can have one answer, more than one answer,...
Can someone help me answers these? These questions can have one answer, more than one answer, or none. Which of the following factors directly affects the distance and speed of a migration of a protein during electrophoresis? - affinity of protein to agarose/polysaccharides - solubility of protein - shape of protein - function of a protein - size of protein (I chose the size of protein, and I got partial wrong 2/4) What is the function of sodium dodecyl sulfate...
a. Which spot corresponds to the protein with the largest molecular weight? b. When pH = 7, what order would the follow...
a. Which spot corresponds to the protein with the largest
molecular weight?
b. When pH = 7, what order would the following peptides elute
from a column filled with cation exchange resin? Size exclusion
column?
Protein 1 – 400 kDa;
10%A 5%E, 5%F, 10% G, 5% H, 10%I, 10%K, 10%L 10%R, 5%P, 5%S, 10%W,
5%Y
Protein 2: 40 kDa
5%A, 5%C, 5%D, 5%E, 5%F, 10%G, 5%I, 10%K, 5%L, 5%M, 5%N, 10%P, 5%R,
5%S, 5%T, 5%V, 5%W,
Protein 3 – 175...
16) At which pH values would two different peptides, one with a pl of 5.9 and...
16) At which pH values would two different peptides, one with a pl of 5.9 and the other with a pl of 9.1, both bind to a cation exchange column? A) pH 3.9 B) pH 7.3 C) pH 10.9 D) None of the above 17) Which type of gel matrix (aka resin) would separate the following proteins using size exclusion chromatography: protein 1 (2,000 Da), protein 2 (7,000 Da), protein 3 (20,000 Da), and protein 4 (90,000 Da)? A) Gel...
Which methods would i use to purify the protein 10 from agbooth?
which methods would i use to purify the protein 10 from
agbooth?
Quit Separation PAGE Fractions Help pH 80K 60K 50K- 40K- 30K- 20K- 5K 10K- 5K 2D-PAGE of initial mixture 4 Record pH Ammoniurm sulfate frectionation Heat treatment Gel filtration ton exchange chromatography 80K- 60K 50K 40K- 30K- 1-Dimensional PAGE 2-Dimensional PAGE M, Abandon scheme and start again 20K Store your material... 10K- 5K Using antibody to protein 10 Free versions of Protein Purification are available for the iPhone...
6. You are given a mixture of proteins that you analyze by standard 2-D electrophoresis, with...
6. You are given a mixture of proteins that you analyze by standard 2-D electrophoresis, with the following results for isoelectric points and apparent molecular weights: protein A (Mr 110,400; pl 4.60), protein B (Mr 10,100; pl 6.93), protein C (Mr 65,200; pI 7.84), and protein D (M 25,000; pI 8.15) a. After the 2-D separation, which protein will be in the upper left quadrant of the gel. given that e cathode-proximal end of the isoelectric focusing gel was on...
1. Which is a correct description of the use of separation techniques to separate a dipeptide...
1. Which is a correct description of the use of separation techniques to separate a dipeptide from a pentapeptide? a. the dipeptide emerges faster than the pentapeptide from a gel filtration column b. the dipeptide migrates faster towards the cathode than the pentapeptide on SDS-PAGE c. the dipeptide migrates to a more anodal position than the pentapeptide on electrofocusing d. the dipeptide sediments faster than the pentapeptide in an ultracentrifugal field e. none of these methods would separate the dipeptide...
1.) Describe the goals of a Gel Filtration Chromotography Experiment??? 2.) Explain each key theoretical principle...
1.) Describe the goals of a Gel Filtration Chromotography
Experiment???
2.) Explain each key theoretical principle of a Gel Filtration
Chromotography, and how they help acheive the goal???.
4.) Explain the key equations used in the Gel Filtration
Chromotography experiment and the terms involved in the
equation????
HI im trying to prepare for a lab/report and i have some
questions i could use help with please :) over all having trouble
seeing how everything ties together etc :) thank you...
SIRJE GEL OBJECTIVE: Partial purification of a protein, isocitrate dehydrogenase (IDH), using DEAE ion exchange chromatography....
SIRJE GEL OBJECTIVE: Partial purification of a protein, isocitrate dehydrogenase (IDH), using DEAE ion exchange chromatography. IDH will be eluted from the column using increasing concentrations of KCI. IDH will be tracked using the IDH activity assay and the extent of purification will be analyzed using SDS PAGE Last week we assayed for the activity of the enzyme, isocitrate dehydrogenase, from E.coli strains carrying a plasmid that over-expresses the E. coli IDH gene. To purify proteins from cel extracts, biochemists...
Biochem help 2 14. What would be the net charge on the dipeptide Ser-His at pH-...
Biochem help 2
14. What would be the net charge on the dipeptide Ser-His at pH- 6.04? (Choose the one best answer.) a) 1.5 b) +1; c) +0.5 d) 0 e) -0.5; 15. The pKa of a lysine side chain in a protein ending up on the outside of a globular protein has a different pKa than if the lysine is buried within the interior of a protein. What would be the expected pKa of a side chain of lysine...
a. Which spot corresponds to the protein with the largest
molecular weight?
b. When pH = 7, what order would the following peptides elute
from a column filled with cation exchange resin? Size exclusion
column?
Protein 1 – 400 kDa;
10%A 5%E, 5%F, 10% G, 5% H, 10%I, 10%K, 10%L 10%R, 5%P, 5%S, 10%W,
5%Y
Protein 2: 40 kDa
5%A, 5%C, 5%D, 5%E, 5%F, 10%G, 5%I, 10%K, 5%L, 5%M, 5%N, 10%P, 5%R,
5%S, 5%T, 5%V, 5%W,
Protein 3 – 175...
16) At which pH values would two different peptides, one with a pl of 5.9 and the other with a pl of 9.1, both bind to a cation exchange column? A) pH 3.9 B) pH 7.3 C) pH 10.9 D) None of the above 17) Which type of gel matrix (aka resin) would separate the following proteins using size exclusion chromatography: protein 1 (2,000 Da), protein 2 (7,000 Da), protein 3 (20,000 Da), and protein 4 (90,000 Da)? A) Gel...
which methods would i use to purify the protein 10 from
agbooth?
Quit Separation PAGE Fractions Help pH 80K 60K 50K- 40K- 30K- 20K- 5K 10K- 5K 2D-PAGE of initial mixture 4 Record pH Ammoniurm sulfate frectionation Heat treatment Gel filtration ton exchange chromatography 80K- 60K 50K 40K- 30K- 1-Dimensional PAGE 2-Dimensional PAGE M, Abandon scheme and start again 20K Store your material... 10K- 5K Using antibody to protein 10 Free versions of Protein Purification are available for the iPhone...
6. You are given a mixture of proteins that you analyze by standard 2-D electrophoresis, with the following results for isoelectric points and apparent molecular weights: protein A (Mr 110,400; pl 4.60), protein B (Mr 10,100; pl 6.93), protein C (Mr 65,200; pI 7.84), and protein D (M 25,000; pI 8.15) a. After the 2-D separation, which protein will be in the upper left quadrant of the gel. given that e cathode-proximal end of the isoelectric focusing gel was on...
1.) Describe the goals of a Gel Filtration Chromotography
Experiment???
2.) Explain each key theoretical principle of a Gel Filtration
Chromotography, and how they help acheive the goal???.
4.) Explain the key equations used in the Gel Filtration
Chromotography experiment and the terms involved in the
equation????
HI im trying to prepare for a lab/report and i have some
questions i could use help with please :) over all having trouble
seeing how everything ties together etc :) thank you...
SIRJE GEL OBJECTIVE: Partial purification of a protein, isocitrate dehydrogenase (IDH), using DEAE ion exchange chromatography. IDH will be eluted from the column using increasing concentrations of KCI. IDH will be tracked using the IDH activity assay and the extent of purification will be analyzed using SDS PAGE Last week we assayed for the activity of the enzyme, isocitrate dehydrogenase, from E.coli strains carrying a plasmid that over-expresses the E. coli IDH gene. To purify proteins from cel extracts, biochemists...
Biochem help 2
14. What would be the net charge on the dipeptide Ser-His at pH- 6.04? (Choose the one best answer.) a) 1.5 b) +1; c) +0.5 d) 0 e) -0.5; 15. The pKa of a lysine side chain in a protein ending up on the outside of a globular protein has a different pKa than if the lysine is buried within the interior of a protein. What would be the expected pKa of a side chain of lysine...
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