Combinatorial chemical protein synthesis
In addition, we are actively working in the following areas:
Intrinsically disordered proteins
Nearly one third of eukaryotic proteome is composed of intrinsically disordered proteins or proteins that contain intrinsically disordered domains. Such proteins play many important functional roles in cellular signaling, regulation and recognition. Furthermore, many disease-related proteins are intrinsically disordered. We would like to better understand mechanisms of molecular recognition and complex formation that involve intrinsically disordered proteins and to elucidate their role in protein interaction networks.
Protein misfolding and aggregation
Protein-misfolding diseases (e.g. Alzheimer’s, Parkinson’s diseases and others) affect millions of people worldwide, however, the current understanding of these disorders is incomplete to develop efficient treatments. In these diseases, folded or unstructured proteins undergo conformational isomerization (misfolding) and self-assembly into toxic oligomers and amyloid fibrils. We aim at dissecting the molecular details of such molecular interconversions and identifying molecular targets for designing new drugs and diagnostics against protein-misfolding diseases.
Chemical physics of proteins
In collaboration with Thomas Ebbesen we work towards non-invasive ways to alter protein function. One attractive approach is to employ strong coupling of protein vibrational modes with the vacuum field using photonic cavities. We recently performed proof-of-principle experiments demonstrating quantum strong coupling of protein amide I vibration to a Fabry−Perot mid-infrared cavity and currently are working towards modulating enzyme activity under strong coupling conditions.