Long-range interactions dominate the inverse-temperature dependence of polypeptide hydration free energies

Dheeraj S. Tomar, Michael E. Paulaitis, Lawrence R. Pratt, D. Asthagiri

Research output: Contribution to journalArticlepeer-review

Abstract

Direct, all-atom calculations of the free energy of hydration of aqueous deca-alanine structures — holistically including backbone and side-chain interactions together — show that attractive interactions and the thermal expansion of the solvent explain the inverse temperature signatures that have been interpreted traditionally in favor of hydrophobic mechanisms for stabilizing the structure and function of soluble proteins.

Original languageEnglish (US)
JournalUnknown Journal
StatePublished - Dec 17 2018

Keywords

  • Inverse temperature dependence
  • Long-range interactions
  • Polypeptide hydration free energies

ASJC Scopus subject areas

  • General

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