Just a quick note on protein conformation.  Proteins are not static, like Demis noted.  Proteins are dynamical systems themselves and do not exist as a single stable conformation.  They fluctuate around this equilibrium.  Generally, the changes are relatively small but critical.  However, proteins evolved to exist in multiple stable conformations, each of which having various functions.  <br><br>For instance, we could have a domain in the protein that is hidden and this domain catalyzes some chemical reaction.  Another protein may add a negative charge to a specific atom on a specific amino acid and this changes the stable conformation of the protein, exposing the hidden domain and allowing it to catalyze some chemical reaction as required.<br><br>In many cases, a single protein may exist in many different stable conformations.  To make matters worse, proteins undergo significant modifications that are dynamic themselves.  Different molecules are added to mediate various functions.  These molecules can alter the function, as in the example above.  Moreover, when proteins interact, this can modulate the protein structure.  A simple example is adding tension to the system, a form of mechanical energy, so that when some event happens, it can use that energy to facilitate some physical change in another molecule, RNA for example.<br><br>But this is step one.  However, it should be noted that protein structures still need to be validated.  A prediction does not "solve" protein folding but it will hopefully massively accelerate a wide range of research where a very close structure is sufficient to make scientific progress.