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,
(stuff deleted)
> The crystal structure is a good model of the solution structure with 
> regard to the core structure, but surface features can change considerably.
(stuff deleted)    
>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
(stuff deleted)

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/
|____________________________________________________________________________



More information about the Molmodel mailing list