LATEST NEWS

Tubby

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We identified a previously unknown PIP2 lipid binding site in the barrel-shaped Tubby protein that could help to understand various diseases.

Cool work from our former post-doc Sebastian Thallmair and his colleagues. Now published in Science Advances. DOI: 10.1126/sciadv.abp9471

Foldable Martini

The group of Matysiak has developed a Martini variant for foldable proteins ! Nice work: Sahoo et al. JCTC, in press.

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Martini versus Charmm

From the Risselada lab: a comparison between Martini 2, 3, and Charmm36 on the binding of amphipathic peptides to lipid bilayers. From the abstract: "We observed that Martini 3 qualitatively reproduces experimental trends while producing substantially lower (relative) binding free energies and shallower membrane insertion depths compared to atomistic simulations. In contrast, Martini 2 tends to overestimate (relative) binding free energies." For more details, see: van Hilten et al., JCTC 2022.

Martini perspective

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Not to be missed for Martini aficionados: we wrote a perspective on twenty years of Martini development, describing the history, state-of-the art, and examples of diverse application areas.

"Two decades of Martini: Better beads, broader scope"

Marrink et al., Wires Comput. Mol. Sci.

Nuclear pore complex

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Craving for large Martini's ?

Have a look at this paper, featuring Martini simulations of the nuclear pore complex, featuring hundreds of scaffold proteins embedded in a half-toroidal double membrane !

Mosalaganti et al., Science, 2022. DOI: 10.1126/science.abm950