Dear Sir/Madam,
I tried to study the effect of mutation for a protein. I tried several starting geometries and protocols. I also found the rmsd of wild type protein (~3 A) larger than that of mutant one (~2A), compare to the starting geometry after the minization (before md starts). Is this difference acceptable? I plot the rms over time for the two systems, I found the rmsd of the wild type is consistently higher than that of mutant one. But should I comment on the difference between 3 A vs. 2 A? Is the different too small to be sound biologically?
Does 3A rms acceptable in general?
How can I confirm if the differences in rms is because of my mistakes or the real biological differences of the two proteins?
Bst regards,
CAt
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Received on Wed Jul 08 2009 - 08:34:49 PDT
