Effects of end-group termination on salting-out constants for triglycine

Jana Hladílková, Jan Heyda, Kelvin B. Rembert, Halil I. Okur, Yadagiri Kurra, Wenshe R. Liu, Christian Hilty, Paul S. Cremer, Pavel Jungwirth

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


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 previous 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 because they are strongly influenced by interactions of the ions with the negatively charged C terminus.

Original languageEnglish (US)
Pages (from-to)4069-4073
Number of pages5
JournalJournal of Physical Chemistry Letters
Issue number23
StatePublished - Dec 5 2013

All Science Journal Classification (ASJC) codes

  • General Materials Science
  • Physical and Theoretical Chemistry


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