Reproducibility in the unfolding process of protein induced by an external electric field

The dynamics of proteins are crucial for their function. However, commonly used techniques for studying
protein structures are limited in monitoring time-resolved dynamics at high resolution. Combining electric
fields with existing techniques to study gas-phase proteins, such as single particle imaging using freeelectron
lasers and gas-phase small angle X-ray scattering, has the potential to open up a new era in
time-resolved studies of gas-phase protein dynamics. Using molecular dynamics simulations, we identify
well-defined unfolding pathways of a protein, induced by experimentally achievable external electric
fields. Our simulations show that strong electric fields in conjunction with short-pulsed X-ray sources
such as free-electron lasers can be a new path for imaging dynamics of gas-phase proteins at high
spatial and temporal resolution.