Our main research goals are to develop mass-spectrometry-based methods and apply them in collaborations to understand proteins, their solvent accessibility, aggregation, interfaces, affinities of binding, and their folding. This area of research is often termed “structural proteomics”. The meaning of structure is illustrated in the figure below. Atomic resolution structure is obtained by X-ray crystallography, Cryo-EM and NMR, whereas structural proteomics provides solvent acccessible surface areas and changes in stucture owing to ligand binding, mutation, or changes in media. Low resolution approaches (e.g., dynamic light scattering , CD, IR) also yield structural information but little site-specific information. 

We emphasize three general problems: (1) amyloid protein aggregation (e.g., Aβ in Alzheimer’s disease), (2) membrane protein conformational changes accompanying interactions with drugs, for example, and (3) viral proteins and their interactions with other proteins and RNA (e.g., Covid, Ebola infections). Additionally, we are extending our methods to understand structural changes in mRNA, motivated by the new mRNA vaccines.