Martini 2.2


Try out now! Martini 2.2: Improved parameters for the protein force field

D.H. de Jong, G. Singh, W.F.D. Bennett, C. Arnarez, T.A. Wassenaar, L.V. Schäfer, X. Periole, D.P. Tieleman, S.J. Marrink
Improved Parameters For The Martini Coarse-Grained Protein Force Field, J. Chem. Th. Comp, 9:687–697, 2013. DOI:10.1021/ct300646g


Curious? Go here for downloading the Martinize script which now features a beta release of Martini 2.2. Any feedback is appreciated so we can further improve the model.

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Dimerization of GPCRs


First report on the free energy surface of membrane protein dimerization

X. Periole, A.M. Knepp, T.P. Sakmar, S.J. Marrink, T. Huber.
Structural determinants of the supra-molecular organization of
G protein-coupled receptors in bilayers.
JACS, 134 (26), pp 10959–10965. abstract

Read more: Dimerization of GPCRs


A new script to generate both structure and topology files for coarse grain proteins has been released: Generating input files for a Martini simulation from an atomistic structure takes only one step!

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Critical testing of Martini

Dimerization of Martini amino acids comparable to atomistic force fields

D.H. de Jong, X. Periole, S.J. Marrink. Dimerization of amino acid side chains: lessons from the comparison of different forcefields. JCTC, 8:1003–1014, 2012. abstract

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Membrane protein sequestering

Martini in Naturerissel-domain

G. van den Bogaart, K. Meyenberg, H.J. Risselada, et al., R. Jahn
Membrane protein sequestering by ionic protein–lipid interactions.
Nature, doi:10.1038/nature10545

Read more: Membrane protein sequestering