Life takes place through the concerted flow of numerous biological processes.
The specificity and function of a given protein is determined by its unique three-dimensional structure and by motions of groups of atoms within this scaffold. We are interested in observing changes in atomic level structure and dynamics induced by perturbations, such as ligand binding or phosphorylation, that are associated with these transient interactions. Such information provides insights into unanswered questions regarding the origins of binding energy and the mechanisms by which protein function is regulated. These questions are critical in practical endeavors such as drug design and protein engineering. Our research involves the application of multidimensional NMR spectroscopy to investigate the structure and dynamics of proteins in different functional states.