Matteo Giani joined the Computational Biophysics group in December 2012 as a PhD candidate.
He obtainined his master's degree in November 2012 in biophysics at Universita' degli studi di Milano (Milano, Italy),
completing his master thesis at Sissa, (Trieste, Italy) under the supervision of Angelo Rosa.
Prior to that, he worked in the bioinformatics group lead by Manuela Sironi at Scientific Institute IRCSS E.Medea (Bosisio Parini, Italy).
He also worked as a system administrator in a computer lab, LCM (University of Milan) and has quite a strong background in Linux.
His research experience includes Monte Carlo and Brownian Dynamics simulations of coarse-grain models for polymers and biomolecules.
Clathrin is an eukaryotic protein with a peculiar pinwheel-like shape composed of three identical legs connected at a common hub.
It forms coats for cargo transport vesicles budding from the cytoplasmatic membrane as well as flat,
hexagonal lattices against the membrane surface.
Clathrin does not bind directly to either the membrane or the cargo but is rather
linked to the membrane surface by adaptor proteins such as AP2,
that also enable the triskelions to self-assemble in bulk under the right conditions.
In several preceding papers,
clathrin were modeled as rigid patchy particles.
We developed a matching coarse grained model for adaptor proteins and studied
in detail the mechanisms leading to the creation of clathrin cages in bulk through
both MC simulations and theory.
We are now developing a coarse grained model of a membrane to be used in BD simulations, to investigate clathrin's ability to self-assemble near the membrane surface.