Computational study of the stability of the miniprotein trp-cage, the GB1 β-hairpin, and the AK16 peptide, under negative pressure

Harold W. Hatch, Frank H. Stillinger, Pablo G. Debenedetti

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

Although hot, cold, and high pressure denaturation are well characterized, the possibility of negative pressure unfolding has received much less attention. Proteins under negative pressure, however, are important in applications such as medical ultrasound, and the survival of biopoloymers in the xylem and adjacent parenchyma cells of vascular plants. In addition, negative pressure unfolding is fundamentally important in obtaining a complete understanding of protein stability and naturally complements previous studies of high pressure denaturation. We use extensive replica-exchange molecular dynamics (REMD) simulations and thermodynamic analysis to obtain folding/unfolding equilibrium phase diagrams for the miniprotein trp-cage (α-structure, 20-residue), the GB1 β-hairpin (β-structure, 16-residue), and the AK16 peptide (α-helix, 16-residue). Although the trp-cage is destabilized by negative pressure, the GB1 β-hairpin and AK16 peptide are stabilized by this condition.

Original languageEnglish (US)
Pages (from-to)7761-7769
Number of pages9
JournalJournal of Physical Chemistry B
Volume118
Issue number28
DOIs
StatePublished - Jul 17 2014

All Science Journal Classification (ASJC) codes

  • Materials Chemistry
  • Surfaces, Coatings and Films
  • Physical and Theoretical Chemistry

Fingerprint

Dive into the research topics of 'Computational study of the stability of the miniprotein trp-cage, the GB1 β-hairpin, and the AK16 peptide, under negative pressure'. Together they form a unique fingerprint.

Cite this