title: De novo design of stable α-helices.
abstract: 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.
authors.affiliation: Department of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, NRC Kurchatov Institute, Gatchina, 188300, Russia.
authors.forename: Alexander
authors.initials: A
authors.lastname: Yakimov
authors.forename: Georgy
authors.initials: G
authors.lastname: Rychkov
authors.forename: Michael
authors.initials: M
authors.lastname: Petukhov
mesh_terms: D000465:Algorithms; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D055550:Protein Stability; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides