Structural biology should be computable.
It's been known for over 40 years that
protein structures are completely determined by their amino acid sequences.
For almost all protein structures and all protein-protein complexes,
the experimentally observed structures and
conformations are almost certain to correspond to global free energy minima.
So, it should be possible to predict the structures of proteins and
protein-protein complexes readily by
identifying the global free energy minima for a polypeptide chain,
in case of protein structure prediction,
or identifying the global free energy minima for two proteins coming together,
which will be the prediction of protein complexes problem.
If we could do this, it would both be a fundamental test of
our understanding of macromolecular and interactions,
and it would also be huge practical relevance as
the cost of determining protein structures computationally,
would be a small fraction of the cost of
current experimental methods such as X-ray crystallography, and NMR spectroscopy.
But, as you know, today,
structural biology is not computed,
it is primarily experimental science.
And what I'm going to tell you about today is progress
towards making structural biology computable.
The work I'm going to tell you about today is carried out