Coarse Grain Forcefield for Biomolecules 
Lipid organization and dynamics of biologically complex plasma membranes; comparison of on idealized brain to an average membrane mixture.
H.I. Ingólfsson, T.S. Carpenter, H. Bhatia, P.T. Bremer, S.J. Marrink, F.C. Lightstone. Computational Lipidomics of the Neuronal Plasma Membrane. Biophys. J. 113:2271–2280, 2017. open access
For simulation files and parameters, see bbs.llnl.gov/neuronal-membrane-data.html
Current force fields tend to overstabilize protein-protein interactions, and Martini is no exception. A recent paper by the Vattulainen group shows the stickiness is also haunting membrane embedded proteins:
M. Javanainen, H. Martinez-Seara, I. Vattulainen. PLoS ONE 12:e0187936, 2017. https://doi.org/10.1371/journal.pone.0187936
We are working hard to improve the protein-protein interactions in the forthcoming Martini 3.0 force field, featuring a thoroughly recalibrated interaction matrix, with a planned release early 2018.
Our former PhD student Jelger Risselada has performed large scale Martini simulations of SNARE-mediated membrane fusion and teamed up with experimentalists to explain how tethering proteins facilitate opening of the fusion pore. The exciting results are published in Nature:
M. D’Agostino, H.J. Risselada, A. Lürick, C. Ungermann, A. Mayer. A tethering complex drives the terminal stage of SNARE-dependent membrane fusion. Nature, doi:10.1038/nature24469
The group of Tristan Bereau uses truly high-throughput Martini simulations to screen thermodynamic properties of drug-membrane interactions. They establish linear relationships between partitioning coefficients and key features of the potential of mean force, allowing them to predict the structure of the insertion from bulk experimental measurements for more than 400 000 (!!) compounds. Details can be found here:
This is the first paper of a fresh PhD student in our lab (Bart). We are proud to say that we made it to the cover! In this paper we show that we can build intial structures for all kind of membrane motives using the CHARMM-GUI interface and the Martini CG force field.
, , , , , , , , , . J. Comput. Chem. 2017, 38, 2354–2363. DOI: 10.1002/jcc.24895
Looking for a way to model foldable Martini proteins? Try Go Martini, a clever combination of Martini and Go potentials developed by the group of Theodorakis. Further details on the method can be found in the publication:
A.B. Poma, M. Cieplak, P.E. Theodorakis, JCTC, 13:1366–1374, 2017. DOI:10.1021/acs.jctc.6b00986