Although often depicted as rigid structures, proteins are highly dynamic
systems, whose motions are essential to their functions. Despite this, it is
difficult to investigate protein dynamics due to the rapid timescale at which
they sample their conformational space, leading most NMR-determined structures
to represent only an averaged snapshot of the dynamic picture. While NMR
relaxation measurements can help to determine local dynamics, it is difficult
to detect translational or concerted motion, and only recently have
significant advances been made to make it possible to acquire a more holistic
representation of the dynamics and structural landscapes of proteins. Here, we
briefly revisit our most recent progress in the theory and use of exact
nuclear Overhauser enhancements (eNOEs) for the calculation of structural
ensembles that describe their conformational space. New developments are
primarily targeted at increasing the number and improving the quality of
extracted eNOE distance restraints, such that the multi-state structure
calculation can be applied to proteins of higher molecular weights. We then
review the implications of the exact NOE to the protein dynamics and function
of cyclophilin A and the WW domain of Pin1, and finally discuss our current
research and future directions