@ARTICLE{Yakimov20141,
author={Yakimov, A. and Rychkov, G. and Petukhov, M.},
title={De novo design of stable α-helices},
journal={Methods in Molecular Biology},
year={2014},
volume={1216},
pages={1-14},
doi={10.1007/978-1-4939-1486-9_1},
note={cited By 6},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84921740210&doi=10.1007%2f978-1-4939-1486-9_1&partnerID=40&md5=65710a7e9cfa8e5cfd033b24d7eca07b},
affiliation={Department of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, NRC Kurchatov Institute, Gatchina, Russian Federation; Saint Petersburg State Polytechnical University, Saint Petersburg, Russian Federation},
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. © Springer Science+Business Media New York 2014.},
author_keywords={Sequence optimization;  Solubility;  Stability;  α-Helix},
funding_details={Russian Foundation for Basic Research12-04-91444-NIH_a},
publisher={Humana Press Inc.},
issn={10643745},
pubmed_id={25213408},
language={English},
abbrev_source_title={Methods Mol. Biol.},
document_type={Article},
source={Scopus},
}

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