CBP Logo

COMPUTATIONAL BIOPHYSICS

UNIVERSITY OF TWENTE
THE NETHERLANDS
welcome
people
highlights
research
publications
education
alumni
twentanglement
Briels trophy
downloads
vacancies
contact us
Briels den Otter Ilie Giani Ahuja Metri
Matteo Giani

Matteo Giani

PhD student

room Carré 4029 Horstring Zuid 115
phone +31 (0)53 489 3545 +31 (0)53 489 3371
e-mail m.giani@utwente.nl
personal website
Matteo Giani

Background

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.

Current research

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.