Protein folding and dynamics

Biomolecules do not exist as a single predefined structure.  They fluctuate about a highly complex multidimensional energy landscape.  Thermodynamic jumps about this energy landscape dictate which conformational substates can be accessed and hence the functional repertoire of the protein, i.e. ligand binding/catalyitc events.

To fully understand biology, and to be able to intervene in biological systems with exceptional precision, it is of critical importance to acquire a complete dynamic profile of system in questions.  This is experimentally challenging and requires the use of highly sophisticated structural and spectroscopic methods.

When considering protein function, the ground state structure determined from crystallographic analysis is only a single, energy averaged representation of an infinitesimally exhaustive collection of states that the protein can assume.  The timescales of interconversion are also highly germane, with fluctuations ranging from subpicosecond to seconds or hours depending on the magnitude of the fluctuation.

For any student of biological science I would implore them to consider the physical aspects of molecular function as opposed to a rough, macroscopic understandings.