In article <199501301540.AB27437 at ux1.cso.uiuc.edu> crebeiz at UIUC.EDU (C. Rebeiz) writes:
> One of the major limitations of homology modeling in plants systems, is
> finding a reference protein with
> a degree of homology = or > than 40% to the target protein. I wonder
> however, about the relationship of a laboratory-grown crystal of a
> membrane-bound solubilized protein to the native protein in situ.
> Constantin A. Rebeiz
> 240 A, PABL
> 1201 W. Gregory
> Univ. Illinois, Urbana, IL 61801
I agree on both counts. Some classes of proteins are very difficult to isolate and crystallize.
This will result in both few template structures for homology modeling and few structures that
can be determined by X-ray crystallography/NMR. The second point is what I meant with the
precision versus 'biologically relevant accuracy' issue in one of my previous posts.
Andrej
