Unraveling the stability of polypeptide helices: critical role of van der Waals interactions.


Journal Article

Folding and unfolding processes are important for the functional capability of polypeptides and proteins. In contrast with a physiological environment (solvated or condensed phases), an in vacuo study provides well-defined "clean room" conditions to analyze the intramolecular interactions that largely control the structure, stability, and folding or unfolding dynamics. Here we show that a proper consideration of van der Waals (vdW) dispersion forces in density-functional theory (DFT) is essential, and a recently developed DFT+vdW approach enables long time-scale ab initio molecular dynamics simulations at an accuracy close to "gold standard" quantum-chemical calculations. The results show that the inclusion of vdW interactions qualitatively changes the conformational landscape of alanine polypeptides, and greatly enhances the thermal stability of helical structures, in agreement with gas-phase experiments.

Full Text

Duke Authors

Cited Authors

  • Tkatchenko, A; Rossi, M; Blum, V; Ireta, J; Scheffler, M

Published Date

  • March 16, 2011

Published In

Volume / Issue

  • 106 / 11

Start / End Page

  • 118102 -

PubMed ID

  • 21469900

Pubmed Central ID

  • 21469900

Electronic International Standard Serial Number (EISSN)

  • 1079-7114

International Standard Serial Number (ISSN)

  • 0031-9007

Digital Object Identifier (DOI)

  • 10.1103/physrevlett.106.118102


  • eng