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Clement Arnarez
Researcher at University of Delaware
Publications - 18
Citations - 2820
Clement Arnarez is an academic researcher from University of Delaware. The author has contributed to research in topics: Respiratory chain & Cardiolipin. The author has an hindex of 13, co-authored 18 publications receiving 2254 citations. Previous affiliations of Clement Arnarez include University of Bordeaux & Universidade Nova de Lisboa.
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Journal ArticleDOI
Improved Parameters for the Martini Coarse-Grained Protein Force Field
Djurre H. de Jong,Gurpreet Singh,W. F. Drew Bennett,Clement Arnarez,Tsjerk A. Wassenaar,Lars V. Schäfer,Xavier Periole,D. Peter Tieleman,Siewert J. Marrink +8 more
TL;DR: Improve some of the bonded terms in the Martini protein force field that lead to a more realistic length of α-helices and to improved numerical stability for polyalanine and glycine repeats.
Journal ArticleDOI
Lipid organization of the plasma membrane.
Helgi I. Ingólfsson,Manuel N. Melo,Floris J. van Eerden,Clement Arnarez,Cesar A. Lopez,Tsjerk A. Wassenaar,Tsjerk A. Wassenaar,Xavier Periole,Alex H. de Vries,D. Peter Tieleman,Siewert J. Marrink +10 more
TL;DR: In this paper, the authors provided a high-resolution view of the lipid organization of a plasma membrane at an unprecedented level of complexity by combining 14 types of headgroups and 11 types of tails asymmetrically distributed across the two leaflets, closely mimicking an idealized mammalian plasma membrane.
Journal ArticleDOI
Dry Martini, a coarse-grained force field for lipid membrane simulations with implicit solvent.
Clement Arnarez,Jaakko J. Uusitalo,Marcelo F. Masman,Helgi I. Ingólfsson,Djurre H. de Jong,Manuel N. Melo,Xavier Periole,Alex H. de Vries,Siewert J. Marrink +8 more
TL;DR: An implicit-solvent version of the popular CG Martini model, nicknamed "Dry" Martini, is introduced, to account for the omitted solvent degrees of freedom, and the nonbonded interaction matrix underlying the Martini force field was reparametrized.
Journal ArticleDOI
Evidence for cardiolipin binding sites on the membrane-exposed surface of the cytochrome bc1.
Clement Arnarez,Jean-Pierre Mazat,Jean-Pierre Mazat,Juan Elezgaray,Juan Elezgaray,Siewert J. Marrink,Xavier Periole +6 more
TL;DR: An extensive set of coarse-grain molecular dynamics simulations aiming at the determination of the preferential interfaces of CLs on the respiratory chain complex III revealed the importance of two subunits of CIII (G and K in bovine heart) for the structural integrity of these internal CL binding sites.
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Identification of cardiolipin binding sites on cytochrome c oxidase at the entrance of proton channels
TL;DR: The results strongly support an involvement of CLs in the proton delivery machinery to CcO, and the ubiquitous nature of CL interactions with the components of the OxPhos suggests that this delivery mechanism might extend to the other respiratory complexes.