In the past decades, single-molecule techniques applied to biomolecules have enriched our understanding of numerous biological systems. Techniques such as AFM, and optical and magnetic tweezers offer the ability to manipulate a single molecule, providing details that no other technique can achieve. In this seminar, I will present advances developed in our laboratory in the past years using single molecule force spectroscopy to understand the role of mechanical forces in the biological function of proteins. Numerous proteins have as a main function acting as mechanical elements that react to an external force in cells. Two prominent examples are titin, a muscle protein thar provide passive elasticity to the muscle; and pilus proteins, a transmembrane protein that bacteria use as mechanical anchor to initiate infection. In the case of titin, I will provide an overview on the evolution of titin mechanics from our ancient ancestor to our modern days, and how titin has modeled the mechanical movement of vertebrates. In the case of pilus, I will describe how the mechanochemical properties of these proteins are essential for bacteria to infect tissues, representing a perfect target to combat infections. Finally, I will present our latest research using a novel approach that utilizes magnetic tweezers to manipulate single cells, which allows a direct correlation between the nanomechanics of proteins and cells.
Instructor: Raul Perez-Jimenez, PhD,
Research Professor, CIC nanoGUNE
Duration: 1 hour
Cost: Free of charge