jdboer at uvic.ca (Johan de Boer) schrieb:
> Hi all,
>> I have a question regarding matching the MW of a protein spot found on
> a 2D gel with that given for that protein by it's identity after
> identification by MALDI. I have seen several instances where there is
> a significant discrepancy, with the gel spot generally being too
> small, such as 50 to 200%. Yet, the matching MALDI fragments of amino
> acid sequence are spread over the whole protein, so the entire
> sequence should be there. What can affect the running of proteins on
> the gels that much? As an example, we find very good matches for
> glutathione S-transferase (covering parts all over the protein) for a
> spot at gel position of 17kD while it is supposed to be 26kD. Others
> are even more off.
You mean SDS or other denaturing gels? Hm, there are some proteins that
are SDS resistant, and only run according to their intrinsic
charge. However, this usually leads to slower migration and thus an
overestimation of the MW. Still one could imagine a protein with a pI
far off the gel pH and a high intrinsic charge.
Bye, Frank
--
> But I don't really see running SETI at Home as practical as Folding at Home. What,
> exactly, would be the benefit of finding intelligent aliens on the other side
> of the galaxy?
Maybe they're broadcasting the principles of protein folding... [from bionet.*]
