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Making lipids very unhappy to discover how they bind to proteins

Stefan, Christopher; Covino, Roberto; (2024) Making lipids very unhappy to discover how they bind to proteins. Journal of Cell Biology , 223 (11) , Article e202410022. 10.1083/jcb.202410022. Green open access

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Abstract

Membrane lipid composition is maintained by conserved lipid transfer proteins, but computational approaches to study their lipid-binding mechanisms are limiting. Srinivasan et al. (https://doi.org/10.1083/jcb.202312055) develop a clever molecular dynamics simulations assay to accurately model lipid-binding poses in lipid transfer proteins.

Type: Article
Title: Making lipids very unhappy to discover how they bind to proteins
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1083/jcb.202410022
Publisher version: http://dx.doi.org/10.1083/jcb.202410022
Language: English
Additional information: © 2024 Stefan and Covino. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
Keywords: Molecular Dynamics Simulation, Protein Binding, Carrier Proteins, Humans, Membrane Lipids, Lipids
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Lab for Molecular Cell Bio MRC-UCL
URI: https://discovery-pp.ucl.ac.uk/id/eprint/10198598
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