In article <2vdk7s$ss at lyra.csx.cam.ac.uk>
Ben Davis, bjd12 at cus.cam.ac.uk writes:
> GIven the amount of work it takes to characterise a denatured state
>fully (I'm primarily talking full NMR assignment + std biochemical
evidence)
>I'm absolutely sure an example of "totally dentaured protein" would get
>published, espc. since there aren't any yet ...
How can you get a full NMR assignment of a fully denatured protein?
There have been many attempts to study denatured proteins by NMR.
The problem is there is no dispersion (in sharp contrast to the folded
state)
in the signals making it impossible to assign them (indicating
that there is little, if any structure). One would expect that if
there were local interactions in the unfolded state, they would
cause dispersion in the chemical shift.
Maybe it would help if you would explain what would satisfy a "totally
denatured protein?"
>______________________________________________________________________
_______
>>Ben Davis,
>MRC Protein Function and Design,
>Cambridge, UK
>______________________________________________________________________
_______
-Ken Prehoda
kenp at nmrfam.wisc.edu
