I think I understand why they would need to be variable in their interaction speed and time. If all transient protein interactions took equal amounts of time to perform their function or all travelled at the same speed, then I don't believe the body could properly function. For example, the various ligands involved in a number of homeostatic systems, such as the HPA axis, need to be different from one another in terms of speed and efficacy because that is what allows them to perform their specific functions. But there are still questions I have about how it all comes together.
Does "far-western blot analysis" mean that there is multiple proteins involved/ it is a quaternary structure that is being examined? I know the a western blot analysis means that proteins are being analyzed, so is far-western just a more specific term?
I wonder how they are able to tell which domains/regions of the two proteins in question are responsible for the binding. It later states that they use DSS for intracellular proteins and BS3 for cell-surface proteins, but I feel like there is not as much specificity. So aside from the new molecular weight of the quaternary structure, what can they infer based on the induced artificial bonds?
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