Thermodynamic uncertainty relations in a linear system

We consider a Brownian particle in harmonic confinement of stiffness $k$, in one dimension in the underdamped regime. The whole setup is immersed in a heat bath at temperature $T$. The center of harmonic trap is dragged under any arbitrary protocol. The thermodynamic uncertainty relations for both position of the particle and current at time $t$ are obtained using the second law of thermodynamics as well as the positive semi-definite property of the correlation matrix of work and degrees of freedom of the system for both underdamped and overdamped cases.Comment: Minor revision, Accepted in EPJ

Growth or Reproduction: Emergence of an Evolutionary Optimal Strategy

Modern ecology has re-emphasized the need for a quantitative understanding of the original 'survival of the fittest theme' based on analyzis of the intricate trade-offs between competing evolutionary strategies that characterize the evolution of life. This is key to the understanding of species coexistence and ecosystem diversity under the omnipresent constraint of limited resources. In this work we propose an agent based model replicating a community of interacting individuals, e.g. plants in a forest, where all are competing for the same finite amount of resources and each competitor is characterized by a specific growth-reproduction strategy. We show that such an evolution dynamics drives the system towards a stationary state characterized by an emergent optimal strategy, which in turn depends on the amount of available resources the ecosystem can rely on. We find that the share of resources used by individuals is power-law distributed with an exponent directly related to the optimal strategy. The model can be further generalized to devise optimal strategies in social and economical interacting systems dynamics.Comment: 10 pages, 5 figure

Accurate and efficient description of protein vibrational dynamics: comparing molecular dynamics and Gaussian models

Current all-atom potential based molecular dynamics (MD) allow the identification of a protein's functional motions on a wide-range of time-scales, up to few tens of ns. However, functional large scale motions of proteins may occur on a time-scale currently not accessible by all-atom potential based molecular dynamics. To avoid the massive computational effort required by this approach several simplified schemes have been introduced. One of the most satisfactory is the Gaussian Network approach based on the energy expansion in terms of the deviation of the protein backbone from its native configuration. Here we consider an extension of this model which captures in a more realistic way the distribution of native interactions due to the introduction of effective sidechain centroids. Since their location is entirely determined by the protein backbone, the model is amenable to the same exact and computationally efficient treatment as previous simpler models. The ability of the model to describe the correlated motion of protein residues in thermodynamic equilibrium is established through a series of successful comparisons with an extensive (14 ns) MD simulation based on the AMBER potential of HIV-1 protease in complex with a peptide substrate. Thus, the model presented here emerges as a powerful tool to provide preliminary, fast yet accurate characterizations of proteins near-native motion.Comment: 14 pages 7 figure

A Stochastic Model for the Species Abundance Problem in an Ecological Community

We propose a model based on coupled multiplicative stochastic processes to understand the dynamics of competing species in an ecosystem. This process can be conveniently described by a Fokker-Planck equation. We provide an analytical expression for the marginalized stationary distribution. Our solution is found in excellent agreement with numerical simulations and compares rather well with observational data from tropical forests.Comment: 4 pages, 3 figures, submitted to PR

A simplified exactly solvable model for beta-amyloid aggregation

We propose an exactly solvable simplified statistical mechanical model for the thermodynamics of beta-amyloid aggregation, generalizing a well-studied model for protein folding. The monomer concentration is explicitly taken into account as well as a non trivial dependence on the microscopic degrees of freedom of the single peptide chain, both in the alpha-helix folded isolated state and in the fibrillar one. The phase diagram of the model is studied and compared to the outcome of fibril formation experiments which is qualitatively reproduced.Comment: 4 pages, 2 figure

On entropy production in nonequilibrium systems

In this paper we discuss the meaning of the Schnakenberg formula for entropy production in non-equilibrium systems. To this end we consider a non-equilibrium system as part of a larger isolated system which includes the environment. We prove that the Schnakenberg formula provides only a lower bound to the actual entropy production in the environment. This is also demonstrated in the simplest example of a three-state clock model.Comment: PDFLaTeX, 16 pages, 5 figure

Recurrent oligomers in proteins - an optimal scheme reconciling accurate and concise backbone representations in automated folding and design studies

A novel scheme is introduced to capture the spatial correlations of consecutive amino acids in naturally occurring proteins. This knowledge-based strategy is able to carry out optimally automated subdivisions of protein fragments into classes of similarity. The goal is to provide the minimal set of protein oligomers (termed ``oligons'' for brevity) that is able to represent any other fragment. At variance with previous studies where recurrent local motifs were classified, our concern is to provide simplified protein representations that have been optimised for use in automated folding and/or design attempts. In such contexts it is paramount to limit the number of degrees of freedom per amino acid without incurring in loss of accuracy of structural representations. The suggested method finds, by construction, the optimal compromise between these needs. Several possible oligon lengths are considered. It is shown that meaningful classifications cannot be done for lengths greater than 6 or smaller than 4. Different contexts are considered were oligons of length 5 or 6 are recommendable. With only a few dozen of oligons of such length, virtually any protein can be reproduced within typical experimental uncertainties. Structural data for the oligons is made publicly available.Comment: 19 pages, 13 postscript figure

Protein Design is a Key Factor for Subunit-subunit Association

Fundamental questions about the role of the quaternary structures are addressed using a statistical mechanics off-lattice model of a dimer protein. The model, in spite of its simplicity, captures key features of the monomer-monomer interactions revealed by atomic force experiments. Force curves during association and dissociation are characterized by sudden jumps followed by smooth behavior and form hysteresis loops. Furthermore, the process is reversible in a finite range of temperature stabilizing the dimer. It is shown that in the interface between the two monomeric subunits the design procedure naturally favors those amino acids whose mutual interaction is stronger. Furthermore it is shown that the width of the hysteresis loop increases as the design procedure improves, i.e. stabilizes more the dimer.Comment: submitted to "Proceedings of the National Academy of Sciences, USA

Entropy production for coarse-grained dynamics

Systems out of equilibrium exhibit a net production of entropy. We study the dynamics of a stochastic system represented by a Master Equation that can be modeled by a Fokker-Planck equation in a coarse-grained, mesoscopic description. We show that the corresponding coarse-grained entropy production contains information on microscopic currents that are not captured by the Fokker-Planck equation and thus cannot be deduced from it. We study a discrete-state and a continuous-state system, deriving in both the cases an analytical expression for the coarse-graining corrections to the entropy production. This result elucidates the limits in which there is no loss of information in passing from a Master Equation to a Fokker-Planck equation describing the same system. Our results are amenable of experimental verification, which could help to infer some information about the underlying microscopic processes