Protein folding problem solved?

Rick Venable rvenable at deimos.cber.nih.gov
Sun Jun 11 13:33:45 EST 1995


On 11 Jun 1995 14:41:15 GMT Simon Brocklehurst (Bioc) pontificated:
> 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.

While that is *generally* true, I suggest that there have been enough
exceptions to advise a little skepticism, and not dogmatically accept
as gospel the notion that a given crystal structure represents the dominant
solution conformation.  Sure, the risk is low for a complete water soluble
globular protein, but increases considerably for isolated subunits or
fragments.  I'd prefer to have independent evidence, and not accept the
equivalence of crystal and solution structures based on a "rule of thumb".

--
Rick Venable                  =====\     |=|    "Eschew Obfuscation"
FDA/CBER Biophysics Lab       |____/     |=|
Bethesda, MD  U.S.A.          |   \  /   |=|  / Not an official statement \
rvenable at deimos.cber.nih.gov       \/    |=|  \  or position of the FDA.  /



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