Lab of Linda K. Nicholson at Cornell University
Life takes place through the concerted flow of numerous biological processes. At the molecular level, this involves highly specific and transient protein-protein and protein-ligand interactions. 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, dynamic intramolecular interactions or environmental triggers, 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. We are focusing on key proteins that have been shown to play important roles in biological processes such as cell cycle control, cell signaling, protein degradation, organelle localization, protein folding and stability, bacterial infection/virulence, etc. Many of these proteins are implicated in disease processes such as Alzheimer's disease, diabetes, AIDS, and cancer.
Most NMR experiments run on a dedicated 600 MHz Varian spectrometer.
Research funded by grants from the National Science Foundation and the National Institute of Health.