Intrinsically disordered proteins (IDPs) play a role in many different biological functions, such as molecular signaling or formation of membraneless organelles.  A common method for studying IDPs is coarse-grained simulations due to large length and timescales that must be probed to simulate phenomena of interest. IDPs are commonly highly charged and can have strong interactions with ions in solution. While most coarse-grained simulations rely on screened electrostatics interactions inspired by Debye-Huckel theory to implicitly capture the effect of ions on, implicit ions are ineffective in properly capturing the effects of the variation of ionic strength and Hofmeister effects. In order to better capture these effects, explicit ions are included in the otherwise implicit solvent, hydrophobicity scale coarse-grained model for implicitly disordered proteins. The inclusion of explicit ions allow for Hofmeister effects of different ion types to be captured by parameterization the Lennard-Jones sigma and epsilon, as well as the hydrophobicity of the ions. This is realized by comparing FRET efficiencies of Prothymosin alpha and starmaker proteins at different ionic strengths. The inclusion of explicit ions allow for effects such as the variation of binding affinity with respect to ionic strength and denaturant effects.  <br/>

Simulation of Hofmeister effects in intrinsically disordered proteins via explicit ion coarse-grained simulations utilizing hydrophobicity scale interactions

2019 Fall National Meeting

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