Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review

Autor: Philipp S. Orekhov, Marine E. Bozdaganyan, Natalia Voskoboynikova, Armen Y. Mulkidjanian, Maria G. Karlova, Anna Yudenko, Alina Remeeva, Yury L. Ryzhykau, Ivan Gushchin, Valentin I. Gordeliy, Olga S. Sokolova, Heinz-Jürgen Steinhoff, Mikhail P. Kirpichnikov, Konstantin V. Shaitan

Publikováno v: Nanomaterials, Vol 12, Iss 3, p 361 (2022)

Amphiphilic copolymers consisting of alternating hydrophilic and hydrophobic units account for a major recent methodical breakthrough in the investigations of membrane proteins. Styrene–maleic acid (SMA), diisobutylene–maleic acid (DIBMA), and re

Externí odkaz: https://doaj.org/article/a167d1deab034ef9be66ba5862c0bb35

Solubilization of artificial mitochondrial membranes by amphiphilic copolymers of different charge

Autor: Janson, Kevin, Zierath, Jennifer, Kyrilis, Fotis L., Semchonok, Dmitry A., Hamdi, Farzad, Skalidis, Ioannis, Kopf, Adrian H., Das, Manabendra, Kolar, Cenek, Rasche, Marie, Vargas, Carolyn, Keller, Sandro, Kastritis, Panagiotis L., Meister, Annette, Sub Membrane Biochemistry & Biophysics, Membrane Biochemistry and Biophysics

Publikováno v: Biochimica et Biophysica Acta-Biomembranes, 1863(12), 1. Elsevier

Certain amphiphilic copolymers form lipid-bilayer nanodiscs from artificial and natural membranes, thereby rendering incorporated membrane proteins optimal for structural analysis. Recent studies have shown that the amphiphilicity of a copolymer stro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f19e8cfb71d542ac7725fef163c3cf81
https://dspace.library.uu.nl/handle/1874/415982

DIBMA nanodiscs keep α-synuclein folded

Autor: Daniel E. Otzen, Jannik Nedergaard Pedersen, Fátima Fonseca, Sandro Keller, Rui M. M. Brito, Regina Adão, Margarida Bastos, Daniela C. Vaz, Carlos H.I. Ramos, Pedro F. Cruz, Frederico Ferreira-da-Silva

Publikováno v: Adão, R, Cruz, P F, Vaz, D C, Fonseca, F, Pedersen, J N, Ferreira-da-Silva, F, Brito, R M M, Ramos, C H I, Otzen, D, Keller, S & Bastos, M 2020, ' DIBMA nanodiscs keep α-synuclein folded ', Biochimica et Biophysica Acta-Biomembranes, vol. 1862, no. 9, 183314 . https://doi.org/10.1016/j.bbamem.2020.183314
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP

α-Synuclein (αsyn) is a cytosolic intrinsically disordered protein (IDP) known to fold into an α-helical structure when binding to membrane lipids, decreasing protein aggregation. Model membrane enable elucidation of factors critically affecting p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a90c86723e23e15ef937955beffc486d
https://hdl.handle.net/10400.8/5233

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