kholdsnare Posted December 4, 2011 Share Posted December 4, 2011 Detailed answers would be appreciated: 1) What is the difference, in terms of data obtained, between Coomassie Blue staining and Western blotting. 2) What kind of important information can be obtained from purifying a protein from the native species itself? 3) Why is it not a good idea to use too much of template DNA for a PCR reaction? Any help would be appreciated, thank you Link to comment Share on other sites More sharing options...
Phi for All Posted December 4, 2011 Share Posted December 4, 2011 Homework? Link to comment Share on other sites More sharing options...
kholdsnare Posted December 4, 2011 Author Share Posted December 4, 2011 no its for a research presentation that i need to give Link to comment Share on other sites More sharing options...
Greippi Posted December 5, 2011 Share Posted December 5, 2011 What, specifically are you stuck on? Link to comment Share on other sites More sharing options...
shaung Posted December 5, 2011 Share Posted December 5, 2011 not goin to answer for you, but: 1. what do you use to help visualise the proteins on a western and isnt used on a coomassie? I.e. what does your secondary antibody bind to in a western? why can you see so many bands in a whole cell lysate coomassie? 2. talk about native protein structure, binding partners, etc. 3. say you have a ball pit full of yellow balls (being your DNA template) and 1 green ball (being your primers) in a room with no gravity, how easy would it be for the green ball to move between the yellow balls to find their specific binding sites. hope this helps! Link to comment Share on other sites More sharing options...
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