NEW
Font size
WorksheetsABT - Electrophoresis review
Total questions: 19
Worksheet time: 12mins
Agarose electrophoresis is used to separate DNA fragments on the basis of which property?
Size
Color
Functions
Chromosomes
In an agarose gel electrophoresis proteins are separated on the basis of ...
net negative charge
net charge and size
net positive charges and size
net positive charge
What is the purpose of using bromophenol blue in the sample buffer?
To ionize the sample.
To monitor the electrophoretic run.
To act as standard control
To adjust the pH of sample.
Why would pH of the running buffer affect the distance travelled by a DNA fragment during agarose electrophoresis
It wouldn't have any effect
It affects charge on the phosphate group and therefore the attraction for cathode
It affects charge on phosphate group and therefore attraction for anode
It hydrolyses the DNA into smaller fragments, affecting band number
How will increasing the concentration of agarose affect how proteins move through the gel in electrophoresis?
All proteins will move faster/further. Order unaffected
Larger proteins will move faster/further. No effect on small. Affects band order.
Large proteins will move slower. No effect on small. Affects band order.
All proteins will move slower/less distance but order unaffected
A student performed a gel electrophoresis experiment. The results are represented in the diagram. Compared to the fragments at the top of the gel, the fragments at the lower end are
larger, and move slower
larger, and move faster
smaller, and move faster
smaller, and move slower
Which of the following statements about SDS-PAGE are false.
Disulfide bonds are cleaved by beta-mercaptoethanol.
Proteins are denatured by the SDS.
Proteins will have a positive charge because of SDS attachment.
Larger proteins move more slowly.
Function of β-mercaptoethanol (thiol) in SDS-PAGE is _______.
To give negative charges to amino acids in the proteins.
For the oxidation of disulfide bonds in the proteins.
For the reduction of disulfide bonds in the proteins.
For breaking hydrogen bonds in the proteins.
In an SDS-PAGE
proteins are denatured by the SDS
proteins have the same charge-to-mass ratio
smaller proteins migrate more rapidly through the gel
all of the above
What would be a suitable visualising stain for SDS page?
lactophenol blue
saffranin
crystal violet
coomassie blue
How are gels calibrated during electrophoresis?
by maintaining constant pH
by maintaining ionic concentration of buffer
using equal volumes of sample
using molecular size markers
In isoelectric focusing, proteins are separated on the basis of their
relative content of positively charged residue only
relative content of negatively charged residue only
size
relative content of positively and negatively charged residue
The electrophoresis technique that used isoelectric focusing is
AGE(Agarose Gel Elecrophoresis)
PFGE (Pulse Field Gel Electrophoresis)
2D- PAGE (Polyacrylamide Gel Electrophoresis)
SDS-PAGE (Sodium dodocyl sulphite)
Which of the following statements about Western Blotting is correct?
The detection of a particular protein by Western Blotting relies on the very specific interaction between the protein and its antibody.
The detection of a particular protein by Western Blotting relies on labelling the protein with a specific dye.
The detection of a particular protein by Western Blotting relies on labelling the antibody with a specific dye.
The detection of a particular protein by Western Blotting relies on the denaturation of the protein.
