Protein-protein interactions play a pivotal role
in the regulation of various cellular processes. The
formation of higher order protein complexes is frequently
accompanied by extensive structural remodeling of
the individual components, varying from domain re-orientation
to induced folding of unstructured elements. Nuclear
Magnetic Resonance (NMR) spectroscopy is a powerful
tool for macromolecular structure determination in
solution. It has the unique advantage of being capable
of elucidating the dynamic behavior of proteins during
the process of recognition. Recent advances in NMR
techniques have enabled the study of significantly
larger proteins and protein complexes. These innovations
have also led to faster and more accurate structure
determination. My research interests focus on the
exploration of molecular recognition and conformation
variability of protein complexes in crucial biomedical
processes using state-of-the-art NMR techniques.
