Andriy Sukhodub wrote:
>> I am interesting if there is any influence of usual
> buffers on protein conformation. My protein perform
> not typical alfa-helix spectra. Are there any
> approaches to make it look pretty? I mean, changing
> the buffer composition or whatever.
If your protein's Far-UV-CD-spectrum doesn't look like "typical
alpha-helix" this means that it does not mainly have alpha-helical
structure. This could be because of the predominance of beta-sheet,
loops or irregular structure, or because it has little structure at
all.
In the latter case, it's easy to induce helical structure, but why
should one want to do this? You get a nice spectrum, but it has
nothing to do with how your protein looks like in the cell or in the
test tube.
Yours, Frank
--
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