Modeling of conformational transitions of fibrillogenic peptide, homologous to beta-domain of human alpha-lactalbumin. Kadochnikov, V., Egorov, V., Shvetsov, A., Kuklin, A., Isaev-Ivanov, V., & Lebedev, D. Crystallography Reports, 61(1):98-105, Maik Nauka-Interperiodica Publishing, 2016. cited By 1![Modeling of conformational transitions of fibrillogenic peptide, homologous to beta-domain of human alpha-lactalbumin [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The behavior of the peptide corresponding to beta domain of human alpha-lactalbumin (GYDTQAIVENNESTEYG, WT) has been simulated by the molecular dynamics method. It is shown that, within the model considered, the monomer of this peptide does not tend to form a stable secondary structure; however, simulation of the behavior of several peptide molecules revealed the occurrence of beta structures due to the formation of intermolecular hydrogen bonds. Since the aforementioned interactions involve the terminal portions of peptides, the influence of the tetrapeptide corresponding to the N-terminal portion of WT, TDYG (R), on the secondary structure has been analyzed. The model calculations show that the interaction of this peptide with WT monomer facilitates formation of beta-structures. It is suggested that peptide R may affect the quaternary structure of WT. © 2016, Pleiades Publishing, Inc.
@ARTICLE{Kadochnikov201698,
author={Kadochnikov, V.V. and Egorov, V.V. and Shvetsov, A.V. and Kuklin, A.I. and Isaev-Ivanov, V.V. and Lebedev, D.V.},
title={Modeling of conformational transitions of fibrillogenic peptide, homologous to beta-domain of human alpha-lactalbumin},
journal={Crystallography Reports},
year={2016},
volume={61},
number={1},
pages={98-105},
doi={10.1134/S1063774516010089},
note={cited By 1},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84955560824&doi=10.1134%2fS1063774516010089&partnerID=40&md5=60272cd63686444584475f84d5406cce},
affiliation={Institute of Physics, Nanotechnology and Telecommunications, St. Petersburg State Polytechnical University, ul. Politekchnicheskaya 29, St. Petersburg, 195251, Russian Federation; St. Petersburg Nuclear Physics Institute, National Research Centre “Kurchatov Institute,”, Orlova Roshcha, Gatchina, Leningrad oblast, 188300, Russian Federation; Research Institute of Influenza, Ministry of Health of the Russian Federation, ul. Prof. Popova 15/17, St. Petersburg, 197976, Russian Federation; Joint Institute for Nuclear Research, ul. Zholio-Kyuri 6, Dubna, Moscow oblast, 141980, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskii per. 9, Dolgoprudnyi, Moscow oblast, 141700, Russian Federation; Institute of Applied Mathematics and Mechanics, St. Petersburg State Polytechnical University, ul. Politekchnicheskaya 29, St. Petersburg, 195251, Russian Federation},
abstract={The behavior of the peptide corresponding to beta domain of human alpha-lactalbumin (GYDTQAIVENNESTEYG, WT) has been simulated by the molecular dynamics method. It is shown that, within the model considered, the monomer of this peptide does not tend to form a stable secondary structure; however, simulation of the behavior of several peptide molecules revealed the occurrence of beta structures due to the formation of intermolecular hydrogen bonds. Since the aforementioned interactions involve the terminal portions of peptides, the influence of the tetrapeptide corresponding to the N-terminal portion of WT, TDYG (R), on the secondary structure has been analyzed. The model calculations show that the interaction of this peptide with WT monomer facilitates formation of beta-structures. It is suggested that peptide R may affect the quaternary structure of WT. © 2016, Pleiades Publishing, Inc.},
correspondence_address1={Kadochnikov, V.V.; Institute of Physics, Nanotechnology and Telecommunications, St. Petersburg State Polytechnical University, ul. Politekchnicheskaya 29, Russian Federation; email: toizeg@gmail.com},
publisher={Maik Nauka-Interperiodica Publishing},
issn={10637745},
language={English},
abbrev_source_title={Crystallogr. Rep.},
document_type={Article},
source={Scopus},
}
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