@CONFERENCE{Vashchenkov2014,
author={Vashchenkov, V.E. and Fedoseev, A.I. and Petukhov, M.G. and Khavinson, V.K. and Savvateeva-Popova, E.V. and Lushnikov, S.G.},
title={Study of low-frequency dynamics of short peptides by Brillouin light scattering and Monte-Carlo global energy minimization},
journal={Journal of Physics: Conference Series},
year={2014},
volume={572},
number={1},
doi={10.1088/1742-6596/572/1/012015},
art_number={012015},
note={cited By 1; Conference of 16th Russian Youth Conference on Physics and Astronomy, PhysicA.SPb 2013 ; Conference Date: 23 October 2013 Through 24 October 2013;  Conference Code:109566},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84919459116&doi=10.1088%2f1742-6596%2f572%2f1%2f012015&partnerID=40&md5=d54ee3ccdf36516aef783201ce70239a},
affiliation={Ioffe Physical Technical Institute, St.Petersburg, Russian Federation; St.Petersburg State University, St.Petersburg, Russian Federation; St.Petersburg State Polytechnical University, St.Petersburg, Russian Federation; Petersburg Institute of Nuclear Physics, Gatchina, Leningrad district, Russian Federation; Pavlov Institute of Physiology, St.Petersburg, Russian Federation},
abstract={Brillouin light scattering studies of the behavior of hypersound velocity in solutions of short peptides Asp-Ser, Glu-Asp-Arg, Ala-Glu-Asp-Leu with widely varying concentrations at temperatures ranging from 295 to 360K are presented. As shown by analysis of experimental data and molecular simulation, the dipeptide Asp-Ser is characterized by formation of dimers which decompose at high temperatures. High-concentration solutions of tri- and tetrapeptides form aggregates at high temperatures which are preserved on cooling. © Published under licence by IOP Publishing Ltd.},
funding_details={Russian Foundation for Basic Research12-04-01737-?},
editor={Averkiev N.S., Sokolovskii G.S., Poniaev S.A.},
sponsors={},
publisher={Institute of Physics Publishing},
issn={17426588},
language={English},
abbrev_source_title={J. Phys. Conf. Ser.},
document_type={Conference Paper},
source={Scopus},
}

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As shown by analysis of experimental data and molecular simulation, the dipeptide Asp-Ser is characterized by formation of dimers which decompose at high temperatures. High-concentration solutions of tri- and tetrapeptides form aggregates at high temperatures which are preserved on cooling. © Published under licence by IOP Publishing Ltd.},\r\nfunding_details={Russian Foundation for Basic Research12-04-01737-?},\r\neditor={Averkiev N.S., Sokolovskii G.S., Poniaev S.A.},\r\nsponsors={},\r\npublisher={Institute of Physics Publishing},\r\nissn={17426588},\r\nlanguage={English},\r\nabbrev_source_title={J. Phys. Conf. Ser.},\r\ndocument_type={Conference Paper},\r\nsource={Scopus},\r\n}\r\n\r\n","author_short":["Vashchenkov, V.","Fedoseev, A.","Petukhov, M.","Khavinson, V.","Savvateeva-Popova, E.","Lushnikov, S."],"editor_short":["Averkiev N.S., S. 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