NMR is the method of choice for investigation of disordered and partially folded proteins. There is a growing recognition that the disordered states of proteins play significant roles in important life processes. In the absence of fixed structure, antibodies, chaperones, and transport proteins and proteolysis machinery of the cell recognize proteins and peptides. Nascent structure in the unfolded state is known to impact pathologies associated with protein folding, ligand binding processes, mutations affecting protein stability and amyloid diseases.
The facility provides nuclear magnetic resonance (NMR) instrumentation primarily for the investigation of the structure and dynamics of biological molecules. The facility consists of a Varian Unity Inova 600 MHz NMR spectrometer capable of state-of-the-art solution NMR experiments.
Basic 1D and 2D NMR applications can be employed for assessing sample purity, chemical changes, binding events and the effects of mutations. More involved multidimensional NMR applications can be implemented for protein structure determination and dynamics investigations. The faculty associated with the NMR core has significant expertise in protein NMR applications aimed at investigating biologically relevant proteins with disordered structure. NMR is ideal for this purpose since protein possessing flexible regions is often difficult or impossible to structurally characterize crystallographically. NMR is uniquely suited to examine changes in the conformation, structure and mobility of proteins using solution conditions closely approximating the biological environment.