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Hi, <br>
<br>
when performing enzymatic assays, we look at triplicates and we can
observe some degree of variation between experimental triplicates
(also between biological triplicates but no exactly the topic is
this question). Sometimes, I even wonder how homogeneous my purified
protein is in the tube, and if I pipet a true homogeneous solution.
<br>
<br>
When we observe the same solution under the microscope, is it the
same population of particles in 2D/3D classes and in the test tube?
<br>
If we see 40% of conformation A, and 60% of conformation B in
initial/crude 3D classification, can we make the claim that it
represents the actual population as in lipuid? <br>
I was also wondering if conformation A and B would enter foilholes
similarly or if some conformations enter holes more preferentially?
<br>
<br>
I couldn't find litterature on the matter, but I image it's been
looked at; could you point me to the right refences? <br>
<br>
This discussion on micro-domains in solution, or micro-concentration
of particles in liquid, becomes more vivid when using pico-liters
type of deposition on grids as we see coming (spotiton, etc...).
Should we then collect 3 grids to link to structural enzymology?<br>
<br>
Looking forward to your comments. <br>
Best<br>
Vincent <br>
<br>
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<p class="p1"><span class="s1">Vincent Chaptal, PhD</span></p>
<p class="p1"><span class="s1">Director of GdR APPICOM</span></p>
<p class="p1"><span class="s1">Drug Resistance and Membrane
Proteins Lab</span></p>
<p class="p2"><span class="s1"></span><br>
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