Abstract
The effect of the neglect of electronic polarization, on the relative stability of different conformations of a model peptide in a nonpolar environment, has been investigated. Configurations generated in molecular dynamics simulations of polyalanine (ACE-ALA15-NH2) in cyctohexane were analyzed in terms of a nonmutual polarization model. The work clearly demonstrates that the stability of conformations which have an enhanced electric field, such as is generated by the formation of a helix dipole, can be significantly underestimated by the neglect of the effects of electronic polarization in weakly polar or nonpolar solvents.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 12830-12833 |
| Number of pages | 4 |
| Journal | Journal of Physical Chemistry B |
| Volume | 106 |
| Issue number | 49 |
| DOIs | |
| State | Published - Dec 12 2002 |
| Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Physical and Theoretical Chemistry
- Surfaces, Coatings and Films
- Materials Chemistry
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Cite this
Soto, P., & Mark, A. E. (2002). The effect of the neglect of electronic polarization in peptide folding simulations. Journal of Physical Chemistry B, 106(49), 12830-12833. https://doi.org/10.1021/jp026526i