Probing the Impact of Polymer Hydrophobicity on Solution and Hydrated Surface Conformation*

Sequence controlled polypeptoids provide a valueable platform for systematic study of molecular level changes in polymer patterning and chemistry; however limitations in our understanidng of sequence effects on polymer conformation and challenges in modeling polypeptoids persist. In this work, distributions of end-to-end distances calculated with molecular dynamics (MD) simulations are compared to those obtained experimentallly via Double Electron Electron Resonance (DEER) spectroscopy. This pulsed electron paramagnetic resonance technique determines a distribution of distances between spin labels placed at each end of a polymer chain, providing insight on sequence-conformation relationships and validation of exisiting simulation force fields. Together, MD and DEER provide a methodology for understanding the impact of polymer sequence and chemistry on polymer conformation as well as confidence in MD predicition of other properties, such as local hydration dynamics at polymer surfaces.