IBMB SEMINAR, FRIDAY 8th. 10:00h | Dr HECTOR GARCIA

Summary
During my scientific career, I have been devoted to understanding how function, stability, and interactions interconnect with the structure and sequence of proteins. In my Ph.D., I combined experimental and bioinformatics approaches to address the design of hyper-stable tailor-made enzymes. In my postdoc, in the Structural Biology Department of the Weizmann Institute, I developed a broad research direction aimed at characterizing the potential of mutations to create promiscuous self-interactions. Briefly, I selected twelve distinct proteins to ascertain the generality of my results, and I undertook a comprehensive characterization of the impact of mutations on their structure and their capacity to self-interact in vitro and in vivo. Through this research, I demonstrated that point mutations at the protein surface frequently create new self-interaction patches that can drive the proteins’ infinite folded-state self-assembly. As an independent researcher, I aim to grasp the sequence determinants and the biophysical mechanisms by which proteins form supramolecular assemblies. My long-term goal is to elucidate the role of supramolecular assemblies in evolution and disease and harness their potential for biotechnological applications.