Towards biomolecular optomechanics

Proteins are the fundamental building block of life. They catalyse almost all chemical reactions in the body, drive the replication of genetic material, and are fundamental to our immune system, among many other important roles.

The 2024 Nobel Prize in Chemistry was awarded for understanding of the structure of individual protein. However, their function is determined not only by structure by, more importantly, but dynamics – how the protein moves through different conformations. Tools to understand protein dynamics are remarkably limited: molecular simulations face immense challenges with predictive modelling at biologically relevant timescales, while real-time measurements are typically limited to millisecond speeds, far below the characteristic speeds of protein motions. To resolve these challenges, my laboratory is developing biomolecular optomechanical tools: nanoscale optical cavities capable of rapid measurement and control of the dynamics of single proteins. In this presentation I will discuss or recent progress, demonstrating the first all-optical single protein traps, observing single protein binding dynamics at sub-microsecond speeds, modelling optomechanical control of protein confirmational changes, and our first steps towards realising this optomechanical control. Our hope is that these methods will enable a new class of tools to understand the role of dynamics in protein function, advancing our understanding of the molecular origins of disease, our ability to design drugs, and our ability to engineer artificial enzymes to purpose.