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Postby forest123 » Tue Oct 19, 2010 2:50 pm

A researcher made two batches of small, 20 um (micrometer) diameter plastic spheres. One batch was made of red plastic, the other of blue plastic. Red plastic spheres were incubated in a solution of purified cadherin IMPs and the blue spheres were incubated with the protein L1. Both cadherin and L1 are normally IMPs but both attached well to the plastic spheres. Red and blue plastic spheres were mixed and left undisturbed for 12 hours in a liquid medium. At the end of the incubation the spheres were aggregated into a large clump. The red spheres were found in the center of this clump and the blue spheres were found on the outer part of the clump, surrounding the core of red spheres.
Next, a solution of cadherin IMPs was treated with protease enzymes until the cadherins were entirely broken up into small peptides (short fragments of the cadherin proteins). These fragments were added to a mixture of red and blue spheres coated with intact cadherin and L1 as above. But this time, after 12 hours of incubation, the blue spheres were found at the center of the aggregate with the red spheres surrounding them.
Explain how these two different patterns arose during incubation in the presence and absence of cadherin fragments.
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Postby JackBean » Thu Oct 21, 2010 6:08 am

I think you should look into how exactly these proteins bind to each other

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