Nonlinear wave trains in three-strand α-helical protein models

C. B. Tabi, J. C. Mimshe Fewu, H. P. Ekobena Fouda, A. Mohamadou, T. C. Kofané

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

Realistic models of α-helix proteins are composed of three covalently-bonded strands, each of which is made of hydrogen-bonded peptide units. The modulational instability analysis of such complex molecular systems is carried out in this work. We show that the exciton-vibron coupling parameter contributes to the explosion and expansion of instability regions. The right choice of the modulational instability parameters leads to the formation of excitonic modulated pulse-like structures. It is argued that covalent bonds are compressed during the process of energy transport, while hydrogen bond oscillations display regular trains of breather-like objects. We also argue that the probable way of energy transport, from modulational instability, is through hydrogen bonds.

Original languageEnglish
Article number374
JournalEuropean Physical Journal B
Volume86
Issue number9
DOIs
Publication statusPublished - Sep 1 2013

All Science Journal Classification (ASJC) codes

  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics

Fingerprint Dive into the research topics of 'Nonlinear wave trains in three-strand α-helical protein models'. Together they form a unique fingerprint.

Cite this