Dynamics of isolated apolipoprotein B-100 (apoB-100) as a function of temperature
Low-density lipoproteins (LDL) are macromolecular assemblies of phospholipids, cholesterol and fat, stabilized by a glycoprotein. We propose to investigate here the molecular dynamics of the protein moiety of LDL; apolipoprotein B-100 (apoB-100), under temperature, lipid-free in the presence of detergents or stabilized by amphiphilic peptides. ApoB-100 is involved in the cellular uptake of LDL, thus deeply linked to LDL biological role. This project aims to provide new information about the molecular dynamics of lipid-free apoB-100, which has never been measured before and that will be combined with future structure determination from cryo-electron microscopy (cryo-EM). In cryo-EM, phospholipid mimicking peptides are added to stabilize the highly flexible structure of apoB-100 : comparison between dynamics of apoB-100 with and without peptides by the means of incoherent neutron scattering is then needed to quantify the stabilisation effect. By gathering all data, we expect to obtain a more comprehensive picture of the structure and dynamics of apoB-100, to relate with LDL functionality.
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CISSE Aline; KORNMUELLER Karin; PETERS Judith and PRASSL Ruth. (2020). Dynamics of isolated apolipoprotein B-100 (apoB-100) as a function of temperature. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-870
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