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

被引:1
|
作者
Volynsky, P. E. [1 ]
Alekseeva, A. S. [1 ]
Boldyrev, I. A. [2 ]
机构
[1] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117871, Russia
[2] Russian Acad Sci, Frumkin Inst Phys Chem & Electrochem, Moscow 117997, Russia
基金
俄罗斯科学基金会;
关键词
PHOSPHOLIPASE A(2) ENZYMES; ACETYLCHOLINESTERASE; BILAYER;
D O I
10.1134/S0021364024600460
中图分类号
O4 [物理学];
学科分类号
0702 ;
摘要
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 approximate to 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.
引用
收藏
页码:643 / 648
页数:6
相关论文
共 50 条
  • [31] Controlling lipid membrane conformations on nanograting structured supports
    Peng, Po-Yu
    Chiang, Po-Chieh
    Chao, Ling
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2014, 248
  • [32] Molecular Interaction between kisspeptin decapeptide analogs and a lipid membrane
    Lee, Ju Yeon
    Moon, Jung Sun
    Eu, Young-Jae
    Lee, Chul Won
    Yang, Sung-Tae
    Lee, Seung Kyu
    Jung, Hyun Ho
    Kim, Ha Hyung
    Rhim, Hyewhon
    Seong, Jae Young
    Kim, Jae Il
    ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2009, 485 (02) : 109 - 114
  • [33] Interaction potentials between lipid membrane coated colloidal particles
    Groves, JT
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2005, 230 : U1046 - U1047
  • [34] INTERACTION BETWEEN PROTEIN AND LIPID - FOCUSED ON SURFACE BEHAVIOR
    YAMANO, Y
    JOURNAL OF THE JAPANESE SOCIETY FOR FOOD SCIENCE AND TECHNOLOGY-NIPPON SHOKUHIN KAGAKU KOGAKU KAISHI, 1992, 39 (02): : 203 - 208
  • [35] Lipid Segregation and Membrane Budding Induced by the Peripheral Membrane Binding Protein Annexin A2
    Druecker, Patrick
    Pejic, Milena
    Galla, Hans-Joachim
    Gerke, Volker
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2013, 288 (34) : 24764 - 24776
  • [36] How Instantaneous Lipid Flows Influence Membrane Protein Diffusion
    Goose, Joseph E.
    Chavent, Matthieu
    Sansom, Mark S. P.
    BIOPHYSICAL JOURNAL, 2013, 104 (02) : 426A - 426A
  • [37] Determining the Free Energy of Membrane Protein Dimerization in Lipid Bilayers
    Krishnamani, Venkatramanan
    Mersch, Kacey
    Chadda, Rahul
    Chadda, Ankita
    Robertson, Janice
    BIOPHYSICAL JOURNAL, 2015, 108 (02) : 39A - 39A
  • [38] Influence of peripheral membrane proteins on nanoparticle interaction with model cell membranes
    Pedersen, Joel
    Melby, Eric
    Kuech, Thomas
    Mensch, Arielle
    Torelli, Marco
    Vartanian, Ariane
    Murphy, Catherine
    Hamers, Robert
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2016, 252
  • [39] Probing the influence of transmembrane peptide charge on its interaction with lipid membrane
    Thakur, Garima
    Uday, Arunima
    Roos, Wouter
    Cwiklik, Lukasz
    Cebecauer, Marek
    Hof, Martin
    Jurkiewicz, Piotr
    Melcrova, Adela
    EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2023, 52 (SUPPL 1): : S162 - S162
  • [40] Influence of Free Fatty Acids on Lipid Membrane-Nisin Interaction
    Saitta, Francesca
    Motta, Paolo
    Barbiroli, Alberto
    Signorelli, Marco
    La Rosa, Carmelo
    Janaszewska, Anna
    Klajnert-Maculewicz, Barbara
    Fessas, Dimitrios
    LANGMUIR, 2020, 36 (45) : 13535 - 13544