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If memory serves, many if not most protein association reactions have
very similar bimolecular association rate constants (say within a factor
of 3 or so). I seem to remember something on the order of 10^5
mol^-1 sec^-1, but I'm not sure of that, you'd better look it up.
(Note: this is orders of magnitude smaller than the upper limit
calculated according to Smoluchowski, which does not take into account
the orientational constraints applying to a specific association that
greatly increase the entropic barrier to complex formation.)
Therefore, given the equilibrium dissociation constant you should be able
to estimate the dissociation rate constant to within this level of
uncertainty. <br><br>
Diffusion coefficients are irrelevant.<br><br>
Allen Minton<br><br>
<br>
At 07:59 PM 4/5/2008, Wenta Nikola wrote:<br>
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<font size=2>Dear Colleagues!<br>
In order to make my question more precise, I want to to calculate the
theoretically diffusion-controlled maximum possible k_off rate of a given
dimer based it's kD (from SE run), in combination with a calculated
diffusion coefficient for monomer and dimer by HydroPro.<br>
If anyone had any suggestions how to calculate that k_off rate, I would
be very grateful.<br>
Niko</font> <br><br>
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