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Basile Nguyen

Publications and source records attributed to Basile Nguyen.

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Exponential volume dependence of entropy-current fluctuations at first-order phase transitions in chemical reaction networks

In chemical reaction networks, bistability can only occur far from equilibrium. It is associated with a first-order phase transition where the control parameter is the thermodynamic force. At the bistable point, the entropy production is known to be discontinuous with respect to the thermodynamic force.We show that the fluctuations of the entropy production have an exponential volume-dependence when the system is bistable. At the phase transition, the exponential prefactor is the height of the effective potential barrier between the two fixed-points. Our results obtained for Schl\"ogl's model can be extended to any chemical network.

cond-mat.stat-mech

Stochastic thermodynamics of chemical reactions coupled to finite reservoirs: A case study for the Brusselator

Biomolecular processes are typically modeled using chemical reaction networks coupled to infinitely large chemical reservoirs. A difference in chemical potential between these reservoirs can drive the system into a non-equilibrium steady state (NESS). In reality, these processes take place in finite systems containing a finite number of molecules. In such systems, a NESS can be reached with the help of an externally driven pump for which we introduce a simple model. Crucial parameters are the pumping rate and the finite size of the chemical reservoir. We apply this model to a simple biochemical oscillator, the Brusselator, and quantify the performance using the number of coherent oscillations. As a surprising result, we find that higher precision can be achieved with finite-size reservoirs even though the corresponding current fluctuations are larger than in the ideal infinite case.

cond-mat.stat-mech

Interlinked GTPase cascades provide a motif for both robust switches and oscillators

GTPases regulate a wide range of cellular processes, such as intracellular vesicular transport, signal transduction, and protein translation. These hydrolase enzymes operate as biochemical switches by toggling between an active guanosine triphosphate (GTP)-bound state and an inactive guanosine diphosphate (GDP)-bound state. We compare two network motifs, a single-species switch and an interlinked cascade that consists of two species coupled through positive and negative feedback loops. We find that interlinked cascades are closer to the ideal all-or-none switch and are more robust against fluctuating signals. While the single-species switch can only achieve bistability, interlinked cascades can be converted into oscillators by tuning the cofactor concentrations, which catalyse the activity of the cascade. These regimes can only be achieved with sufficient chemical driving provided by GTP hydrolysis. In this study, we present a thermodynamically consistent model that can achieve bistability and oscillations with the same feedback motif.

physics.bio-ph

Phase transition in thermodynamically consistent biochemical oscillators

Biochemical oscillations are ubiquitous in living organisms. In an autonomous system, not influenced by an external signal, they can only occur out of equilibrium. We show that they emerge through a generic nonequilibrium phase transition, with a characteristic qualitative behavior at criticality. The control parameter is the thermodynamic force, which must be above a certain threshold for the onset of biochemical oscillations. This critical behavior is characterized by the thermodynamic flux associated with the thermodynamic force, its diffusion coefficient, and the stationary distribution of the oscillating chemical species. We discuss metrics for the precision of biochemical oscillations by comparing two observables, the Fano factor associated with the thermodynamic flux and the number of coherent oscillations. Since the Fano factor can be small even when there are no biochemical oscillations, we argue that the number of coherent oscillations is more appropriate to quantify the precision of biochemical oscillations. Our results are obtained with three thermodynamically consistent versions of known models: the Brusselator, the activator-inhibitor model, and a model for KaiC oscillations.

cond-mat.stat-mech

Thermodynamic bounds on the ultra- and infra-affinity of Hsp70 for its substrates

The 70 kDa Heat Shock Proteins Hsp70 have several essential functions in living systems, such as protecting cells against protein aggregation, assisting protein folding, remodeling protein complexes and driving the translocation into organelles. These functions require high affinity for non-specific amino-acid sequences that are ubiquitous in proteins. It has been recently shown that this high affinity, called ultra-affinity, depends on a process driven out of equilibrium by ATP hydrolysis. Here we establish the thermodynamic bounds for ultra-affinity, and further show that the same reaction scheme can in principle be used both to strengthen and to weaken affinities (leading in this case to infra-affinity). We show that cofactors are essential to achieve affinity beyond the equilibrium range. Finally, biological implications are discussed.

q-bio.BM