Salting out constants for triglycine were calculated for a series of Hofmeister salts using molecular dynamics simulations. Three variants of the peptide were considered with both termini capped, just the N-terminus capped, and without capping. The simulations were supported by NMR and FTIR measurements. The data provide strong evidence that earlier experimental values of salting out constants assigned to the fully capped peptide (as previously assumed) should have been assigned to the half-capped peptide instead. Therefore, these values cannot be used to directly establish Hofmeister ordering of ions at the peptide backbone, since they are strongly influenced by interactions of the ions with the negatively charged C-terminus.

Chemistry Department Penn State University University Park PA 16802 USA

Chemistry Department Texas A and M University College Station TX 77843

Institute of Organic Chemistry and Biochemistry Academy of Sciences of the Czech Republic Flemingovo nám 2 16610 Prague 6 Czech Republic

Soft Matter and Functional Materials Helmholtz Zentrum Berlin Hahn Meitner Platz 1 14109 Berlin Germany

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