Abstract
It is well known that the structure of an intrinsically disordered protein (IDP) can be affected by changes in salt concentration as salt ions screen the electrostatic interactions between charged amino acids. Many IPDs, however, contain more uncharged amino acids than charged ones. These acids are not subjected to electrostatic screening, but are influenced by the salting-out effect. Using recent Förster resonance energy transfer data, we have parameterized the salting-out effect into a previously established coarse-grained model.
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