In situ analyses of protein structural changes in health and disease

Protein conformational changes induced by external perturbations or internal cues can profoundly influence protein activity and thus modulate cellular physiology. Mass spectrometry (MS)-based proteomic techniques are routinely used to measure changes in protein abundance, post-translational modification and protein interactors, but much less is known about alterations in protein structures.
Prof. Paola Picotti will present a recently developed structural proteomics method that enables analysis of protein structural changes on a proteome-wide scale and directly in complex biological extracts. She will describe how the new approach is used to study the molecular bases of protein aggregation diseases and shed light on the in situ structures of aggregation-prone proteins. Further, she will present an application of the approach to the identification of protein-small molecule interactions, including allosteric and drug-target interactions. Last, Prof. Paola Picotti will discuss the power and limitations of the new approach and present her vision on the future of proteomics.