(553c) Multiscale Simulations Can Reveal the Effect of Ionic Liquids on Structure and Dynamics of Biomolecules

Rational design of unique solvents and surfaces holds great potential for providing new ways to use biomolecules in engineering applications. Computational models such as molecular dynamics (MD) hold great potential for connecting the atomic scale to the mesoscale for a wide range of problems such as biocatalysis or protein stabilization by ionic liquids (ILs). Unfortunately, severe computational restrictions often limit wide-ranging use of these tools to their full potential. New multiscale modeling algorithms that are based on MD have been developed that can overcome these challenges, dramatically increasing the computer’s viability as a tool for computation-driven discovery. This talk will highlight how we are using simulations to understand the dominant driving forces that lead to unique orientation and conformation at the protein/IL interface.  We will cover both examples of using classical all-atom MD simulations as well as the application of metadynamics to study the thermodynamics of various processes like protein folding, highlighting key findings applied to biomolecule structure, dynamics, domain rearrangement and protein folding. Systems discussed in this talk include both large (i.e, multidomain) proteins and small model peptides.