Electrostatic Interaction In The Unfolded States Of Proteins

With recent recognition that the unfolded states of proteins play important and diverse roles in protein functions, some advances have been made in developing experimental techniques to help decipher residue-specific interactions. Here we present a molecular dynamics simulation based method that allows direct prediction of electrostatic interactions in the unfolded proteins under native conditions. The theoretical prediction is confirmed by measurements of pH-dependent folding free energies of a small model protein HP36.