Speaker
David Lacoste
(ESPCI)
Description
Biological systems make extensive use of reversible
polymerization: key biological functions are accomplished by
biopolymers such as peptides, assembled from amino-acids, or
actin and microtubules, assembled respectively from G-actin
and tubulin monomers. On the theoretical side, such systems
represent an ideal ground to test non-equilibrium
statistical physics and thermodynamics, as illustrated by
the pioneering work of T. Hill.
In this talk, inspired by a recent experimental study on the
metabolism of carbohydrates, we model reversible
polymerization from the point of view of non-equilibrium
thermodynamics. We first consider a closed system and show
that the polymers dynamically evolve towards equilibrium
where detailed balance is satisfied. We then consider open
systems, in which the polymers are in contact with
chemostats, characterized by fixed polymer concentrations of
a given length.
