Structure and stability of chiral beta-tapes: a computational coarse-grained approach

G Bellesia, M V Fedorov, Y A Kuznetsov, E G Timoshenko

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Abstract

We present two coarse-grained models of different levels of detail for the description of beta-sheet tapes obtained from equilibrium self-assembly of short rationally designed oligopeptides in solution. Here we only consider the case of the homopolymer oligopeptides with the identical sidegroups attached, in which the tapes have a helicoid surface with two equivalent sides. The influence of the chirality parameter on the geometrical characteristics, namely the diameter, interstrand distance, and pitch, of the tapes has been investigated. The two models are found to produce equivalent results suggesting a considerable degree of universality in conformations of the tapes.

Original languageEnglish
Article number134901
Pages (from-to)-
Number of pages10
JournalJournal of Chemical Physics
Volume122
Issue number13
DOIs
Publication statusPublished - 1 Apr 2005

Keywords

  • amphiphilic assemblies
  • globular proteins
  • energy landscape
  • helical ribbons
  • sheet peptide
  • folded states

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    Bellesia, G., Fedorov, M. V., Kuznetsov, Y. A., & Timoshenko, E. G. (2005). Structure and stability of chiral beta-tapes: a computational coarse-grained approach. Journal of Chemical Physics, 122(13), -. [134901]. https://doi.org/10.1063/1.1866012