Influence of Lipid Conformations on the Interaction Energy between a Membrane and a Peripheral Protein

Peripheral membrane proteins are temporarily coupled to the surface of a membrane, penetrating into the lipid layer. In this work, it has been shown that the fraction of trans configurations of dihedral angles in hydrophobic chains of lipids decreases in the region of contact of peripheral membrane...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:JETP letters 2024-04, Vol.119 (8), p.643-648
Hauptverfasser: Volynsky, P. E., Alekseeva, A. S., Boldyrev, I. A.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 648
container_issue 8
container_start_page 643
container_title JETP letters
container_volume 119
creator Volynsky, P. E.
Alekseeva, A. S.
Boldyrev, I. A.
description Peripheral membrane proteins are temporarily coupled to the surface of a membrane, penetrating into the lipid layer. In this work, it has been shown that the fraction of trans configurations of dihedral angles in hydrophobic chains of lipids decreases in the region of contact of peripheral membrane proteins with the membrane. This effect differs for different lipid chains and for dihedral angles at different distances from the beginning of a chain. A gosh configuration has a higher energy than a trans configuration. Consequently, the decrease in the fraction of trans configurations leads to an increase in the energy of the chain. The energy of chain conformations for the peripheral membrane protein considered in this work increases by ≈2 kJ/mol. A chain in chain conformations is involved in molecular mechanisms determining the elastic modulus of membranes. The energy stored in a conformation chain can be spent to the desorption of protein from the surface of the membrane and can be considered as a reason why the interaction of peripheral membrane proteins with the membrane is temporal.
doi_str_mv 10.1134/S0021364024600460
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_3064675603</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3064675603</sourcerecordid><originalsourceid>FETCH-LOGICAL-c241t-74e447e2d57f3b6e97f4c6af358e8e9f2906ee401102bff5ca3adf3070e9a50b3</originalsourceid><addsrcrecordid>eNp1UEtLAzEQDqJgffwAbwHPq5NNNtk9SqlaqFhQz0t2d9JuaZM1SZH-e7NU8CAehmHme8zwEXLD4I4xLu7fAHLGpYBcSIBUJ2TCoIJMilKdkskIZyN-Ti5C2AAwVnI1IWZuzXaPtkXqDF30Q9_RqbPG-Z2OvbOBOkvjGuncRvS6HXd0ZtGvDrTB-IVoqaYvuGu8tki17dK4RN8P60Tf0qV3EXt7Rc6M3ga8_umX5ONx9j59zhavT_PpwyJrc8FipgQKoTDvCmV4I7FSRrRSG16UWGJl8gokokjPQ94YU7Sa685wUICVLqDhl-T26Dt497nHEOuN23ubTtYcpJCqkMATix1ZrXcheDT14Pud9oeaQT3GWf-JM2nyoyYkrl2h_3X-X_QN6U12ww</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>3064675603</pqid></control><display><type>article</type><title>Influence of Lipid Conformations on the Interaction Energy between a Membrane and a Peripheral Protein</title><source>Springer Nature - Complete Springer Journals</source><creator>Volynsky, P. E. ; Alekseeva, A. S. ; Boldyrev, I. A.</creator><creatorcontrib>Volynsky, P. E. ; Alekseeva, A. S. ; Boldyrev, I. A.</creatorcontrib><description>Peripheral membrane proteins are temporarily coupled to the surface of a membrane, penetrating into the lipid layer. In this work, it has been shown that the fraction of trans configurations of dihedral angles in hydrophobic chains of lipids decreases in the region of contact of peripheral membrane proteins with the membrane. This effect differs for different lipid chains and for dihedral angles at different distances from the beginning of a chain. A gosh configuration has a higher energy than a trans configuration. Consequently, the decrease in the fraction of trans configurations leads to an increase in the energy of the chain. The energy of chain conformations for the peripheral membrane protein considered in this work increases by ≈2 kJ/mol. A chain in chain conformations is involved in molecular mechanisms determining the elastic modulus of membranes. The energy stored in a conformation chain can be spent to the desorption of protein from the surface of the membrane and can be considered as a reason why the interaction of peripheral membrane proteins with the membrane is temporal.</description><identifier>ISSN: 0021-3640</identifier><identifier>EISSN: 1090-6487</identifier><identifier>DOI: 10.1134/S0021364024600460</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Atomic ; Biological and Medical Physics ; Biophysics ; Configurations ; Lipids ; Membranes ; Modulus of elasticity ; Molecular ; Molecular conformation ; Optical and Plasma Physics ; Particle and Nuclear Physics ; Physics ; Physics and Astronomy ; Proteins ; Quantum Information Technology ; Solid State Physics ; Spintronics</subject><ispartof>JETP letters, 2024-04, Vol.119 (8), p.643-648</ispartof><rights>The Author(s) 2024. ISSN 0021-3640, JETP Letters, 2024, Vol. 119, No. 8, pp. 643–648. © The Author(s), 2024. This article is an open access publication. Russian Text © The Author(s), 2024, published in Pis’ma v Zhurnal Eksperimental’noi i Teoreticheskoi Fiziki, 2024, Vol. 119, No. 8, pp. 624–629.</rights><rights>The Author(s) 2024. ISSN 0021-3640, JETP Letters, 2024, Vol. 119, No. 8, pp. 643–648. © The Author(s), 2024. This article is an open access publication. Russian Text © The Author(s), 2024, published in Pis’ma v Zhurnal Eksperimental’noi i Teoreticheskoi Fiziki, 2024, Vol. 119, No. 8, pp. 624–629. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c241t-74e447e2d57f3b6e97f4c6af358e8e9f2906ee401102bff5ca3adf3070e9a50b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S0021364024600460$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S0021364024600460$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids></links><search><creatorcontrib>Volynsky, P. E.</creatorcontrib><creatorcontrib>Alekseeva, A. S.</creatorcontrib><creatorcontrib>Boldyrev, I. A.</creatorcontrib><title>Influence of Lipid Conformations on the Interaction Energy between a Membrane and a Peripheral Protein</title><title>JETP letters</title><addtitle>Jetp Lett</addtitle><description>Peripheral membrane proteins are temporarily coupled to the surface of a membrane, penetrating into the lipid layer. In this work, it has been shown that the fraction of trans configurations of dihedral angles in hydrophobic chains of lipids decreases in the region of contact of peripheral membrane proteins with the membrane. This effect differs for different lipid chains and for dihedral angles at different distances from the beginning of a chain. A gosh configuration has a higher energy than a trans configuration. Consequently, the decrease in the fraction of trans configurations leads to an increase in the energy of the chain. The energy of chain conformations for the peripheral membrane protein considered in this work increases by ≈2 kJ/mol. A chain in chain conformations is involved in molecular mechanisms determining the elastic modulus of membranes. The energy stored in a conformation chain can be spent to the desorption of protein from the surface of the membrane and can be considered as a reason why the interaction of peripheral membrane proteins with the membrane is temporal.</description><subject>Atomic</subject><subject>Biological and Medical Physics</subject><subject>Biophysics</subject><subject>Configurations</subject><subject>Lipids</subject><subject>Membranes</subject><subject>Modulus of elasticity</subject><subject>Molecular</subject><subject>Molecular conformation</subject><subject>Optical and Plasma Physics</subject><subject>Particle and Nuclear Physics</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Proteins</subject><subject>Quantum Information Technology</subject><subject>Solid State Physics</subject><subject>Spintronics</subject><issn>0021-3640</issn><issn>1090-6487</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><recordid>eNp1UEtLAzEQDqJgffwAbwHPq5NNNtk9SqlaqFhQz0t2d9JuaZM1SZH-e7NU8CAehmHme8zwEXLD4I4xLu7fAHLGpYBcSIBUJ2TCoIJMilKdkskIZyN-Ti5C2AAwVnI1IWZuzXaPtkXqDF30Q9_RqbPG-Z2OvbOBOkvjGuncRvS6HXd0ZtGvDrTB-IVoqaYvuGu8tki17dK4RN8P60Tf0qV3EXt7Rc6M3ga8_umX5ONx9j59zhavT_PpwyJrc8FipgQKoTDvCmV4I7FSRrRSG16UWGJl8gokokjPQ94YU7Sa685wUICVLqDhl-T26Dt497nHEOuN23ubTtYcpJCqkMATix1ZrXcheDT14Pud9oeaQT3GWf-JM2nyoyYkrl2h_3X-X_QN6U12ww</recordid><startdate>20240401</startdate><enddate>20240401</enddate><creator>Volynsky, P. E.</creator><creator>Alekseeva, A. S.</creator><creator>Boldyrev, I. A.</creator><general>Pleiades Publishing</general><general>Springer Nature B.V</general><scope>C6C</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20240401</creationdate><title>Influence of Lipid Conformations on the Interaction Energy between a Membrane and a Peripheral Protein</title><author>Volynsky, P. E. ; Alekseeva, A. S. ; Boldyrev, I. A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c241t-74e447e2d57f3b6e97f4c6af358e8e9f2906ee401102bff5ca3adf3070e9a50b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Atomic</topic><topic>Biological and Medical Physics</topic><topic>Biophysics</topic><topic>Configurations</topic><topic>Lipids</topic><topic>Membranes</topic><topic>Modulus of elasticity</topic><topic>Molecular</topic><topic>Molecular conformation</topic><topic>Optical and Plasma Physics</topic><topic>Particle and Nuclear Physics</topic><topic>Physics</topic><topic>Physics and Astronomy</topic><topic>Proteins</topic><topic>Quantum Information Technology</topic><topic>Solid State Physics</topic><topic>Spintronics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Volynsky, P. E.</creatorcontrib><creatorcontrib>Alekseeva, A. S.</creatorcontrib><creatorcontrib>Boldyrev, I. A.</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>CrossRef</collection><jtitle>JETP letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Volynsky, P. E.</au><au>Alekseeva, A. S.</au><au>Boldyrev, I. A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Influence of Lipid Conformations on the Interaction Energy between a Membrane and a Peripheral Protein</atitle><jtitle>JETP letters</jtitle><stitle>Jetp Lett</stitle><date>2024-04-01</date><risdate>2024</risdate><volume>119</volume><issue>8</issue><spage>643</spage><epage>648</epage><pages>643-648</pages><issn>0021-3640</issn><eissn>1090-6487</eissn><abstract>Peripheral membrane proteins are temporarily coupled to the surface of a membrane, penetrating into the lipid layer. In this work, it has been shown that the fraction of trans configurations of dihedral angles in hydrophobic chains of lipids decreases in the region of contact of peripheral membrane proteins with the membrane. This effect differs for different lipid chains and for dihedral angles at different distances from the beginning of a chain. A gosh configuration has a higher energy than a trans configuration. Consequently, the decrease in the fraction of trans configurations leads to an increase in the energy of the chain. The energy of chain conformations for the peripheral membrane protein considered in this work increases by ≈2 kJ/mol. A chain in chain conformations is involved in molecular mechanisms determining the elastic modulus of membranes. The energy stored in a conformation chain can be spent to the desorption of protein from the surface of the membrane and can be considered as a reason why the interaction of peripheral membrane proteins with the membrane is temporal.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><doi>10.1134/S0021364024600460</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-3640
ispartof JETP letters, 2024-04, Vol.119 (8), p.643-648
issn 0021-3640
1090-6487
language eng
recordid cdi_proquest_journals_3064675603
source Springer Nature - Complete Springer Journals
subjects Atomic
Biological and Medical Physics
Biophysics
Configurations
Lipids
Membranes
Modulus of elasticity
Molecular
Molecular conformation
Optical and Plasma Physics
Particle and Nuclear Physics
Physics
Physics and Astronomy
Proteins
Quantum Information Technology
Solid State Physics
Spintronics
title Influence of Lipid Conformations on the Interaction Energy between a Membrane and a Peripheral Protein
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T16%3A52%3A28IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Influence%20of%20Lipid%20Conformations%20on%20the%20Interaction%20Energy%20between%20a%20Membrane%20and%20a%20Peripheral%20Protein&rft.jtitle=JETP%20letters&rft.au=Volynsky,%20P.%20E.&rft.date=2024-04-01&rft.volume=119&rft.issue=8&rft.spage=643&rft.epage=648&rft.pages=643-648&rft.issn=0021-3640&rft.eissn=1090-6487&rft_id=info:doi/10.1134/S0021364024600460&rft_dat=%3Cproquest_cross%3E3064675603%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=3064675603&rft_id=info:pmid/&rfr_iscdi=true