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.
By: Professor Paola Picotti
Fifteen years ago, Prof.Craik discovered a family of peptides with a structure like no other that is now called cyclotides. As the name suggests, their structure is cyclic and includes an intricate knot. Today, Prof. Craik's group is re-engineering and adapting peptides to create new drugs. The group had also success in using the methodology to create agri-chemicals, helping the industry to produce a world first eco-friendly insecticide.
By: Prof. Dr. David Craik, University of Queensland