De Novo Design of Stable α-Helices

  • Alexander Yakimov
  • Georgy Rychkov
  • Michael Petukhov
Part of the Methods in Molecular Biology book series (MIMB, volume 1216)


Recent studies have elucidated key principles governing folding and stability of α-helices in short peptides and globular proteins. In this chapter we review briefly those principles and describe a protocol for the de novo design of highly stable α-helixes using the SEQOPT algorithm. This algorithm is based on AGADIR, the statistical mechanical theory for helix-coil transitions in monomeric peptides, and the tunneling algorithm for global sequence optimization.

Key words

α-Helix Stability Sequence optimization Solubility 



This work was supported, in part, by grants from the Russian Ministry of Education and Science (grant No. 11.519.11.2002) and from the Russian Foundation of Basic Research (grant No 12-04-91444-NIH_a).


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Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  • Alexander Yakimov
    • 1
    • 2
  • Georgy Rychkov
    • 1
    • 2
  • Michael Petukhov
    • 1
    • 2
  1. 1.Department of Molecular and Radiation Biophysics, Petersburg Nuclear Physics InstituteNRC Kurchatov InstituteGatchinaRussia
  2. 2.Saint Petersburg State Polytechnical UniversitySaint PetersburgRussia

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