Protein folding problem solved?
Simon Brocklehurst Bioc
smb18 at mole.bio.cam.ac.uk
Sun Jun 11 09:41:15 EST 1995
rvenable at deimos.cber.nih.gov (Rick Venable) writes:
>I'll grant that in most cases the interior hydrophobic packing is preserved
>for protein structures determined by both NMR and x-ray,
> The crystal structure is a good model of the solution structure with
> regard to the core structure, but surface features can change considerably.
>All I'm suggesting is that one shouldn't overinterpret a crystal structure
>as *the* solution structure, but it is generally a good model of a low energy
>conformation easily accessible from the distribution of conformations sampled
>in solution. Keep in mind that surface features can be fairly mobile, and
I think you're making quite a bit too much of the differences between
NMR and X-ray structures. Flexibility in solution is usually mirrored
by flexibility in the crystal.
The take-home message to be drawn from comparisons NMR and X-ray
structures is that they're pretty much the same for all parts of the
protein, not just the core.
Of course, the details of dynamic properties of proteins can be
characterised much better by using solution heteronuclear MR techniques
than by using X-ray techniques, but this information isn't incorporated
into 3-D models in an explicit way at present.
| ,_ o Simon M. Brocklehurst,
| / //\, Oxford Centre for Molecular Sciences, Department of Biochemistry,
| \>> | University of Oxford, Oxford, UK.
| \\, E-mail: smb at bioch.ox.ac.uk | WWW: http://www.ocms.ox.ac.uk/~smb/
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