1.As you saw from the video, the kinesin-GFP prep could be tracked because the s
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Question
1.As you saw from the video, the kinesin-GFP prep could be tracked because the samples
were greenish. The GFP fluorophore, the part of the molecule that produces the
fluorescent color, only forms within the intact -barrel (made up of -sheets) of the GFP
molecule. If you were to run an SDS-PAGE gel with this purified protein, would you
expect the band to be green? Why or why not?
For this one all I could find is that the bands are colorless and this type usually uses blue but don't think that is what the teacher is looking for. Both of these questions are based off of a microtubule movement video analysis lab.
2.For each ATP hydrolyzed, kinesin takes a 7 nm step (i.e. it moves 7nm). What is the
Vmax in terms of molecules of ATP/sec?
Explanation / Answer
When a dye is used in SDS PAGE it gives a particular color to indicate the different charged states of dye due to the presence of protein type. This means that one colour may indicate negative ionized state while appearance of another color may indicate neutral or positive state.
In the given case when purified protein is run in SDS PAGE if a dye is used then bands will not give green color but rather will appear as per the dye's charged state. In case no dye is used then bands will appear colourless. The color of the band in SDS PAGE is not determined by the color of protein but rather by the dye used or the method followed.
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