The proteasome is part of a set of cellular machines dedicated to protein degradation. To achieve this, it has a catalytic subunit that forms a chamber where the substrate proteins are degraded. The entrance to this chamber is performed through a narrow pore that only allow unfolded proteins to enter. A second subunit recognizes and unfolds proteins to introduce them into the catalytic chamber. The proteasome uses force to mechanically unfold the proteins and therefore to perform its function, which highlights the importance of the mechanical properties in all kinds of proteins, not just those with mechanical function.
In the laboratory we are interested in studying how the mechanical stability of proteins can affect their unfolding by the proteasome or other components that use forces to unfold proteins. To do so we combine single-molecule force spectroscopy and biochemical analysis as well as molecular dynamics simulations to understand the role of mechanics in this process of great relevance in biology.