We study the dynamics of a heteropolymeric chain relaxing toward a new equilibrium configuration after the action of an external perturbation. We compare the results from Monte Carlo simulations with the results of a Langevin normal-mode decomposition. We discuss, for the sake of comparison, the case of an ordered homopolymeric chain. We discuss the dependence of the relaxation stretching exponent on the system size by studying chains constituted by 15 and 30 points
The “protein structure-function” paradigm, which states that proteins adopt nearly rigid 3-dimension...
Features of the renormalized and twice renormalized Rouse models were examined numerically. Based on...
We use molecular dynamics simulations of the Kremer–Grest (KG) bead–spring model of polymer chains o...
Polymeric and biological disordered materials are characterized by unique dynamical features. Althou...
The relaxation behaviour of various statistical and thermodynamic many body systems like percolating...
Intrinsically disordered proteins (IDPs) access highly diverse ensembles of conformations in their f...
Static disorder has recently been implicated in the non-exponential kinetics of the unfolding of sin...
We study theoretically the behaviour of a system of « living polymers » (polymers that can break and...
11 p.Using molecular dynamic simulations we study the quench of a homopolymer chain into a poor solv...
The Langevin dynamics of a self-interacting chain embedded in a quenched random medium is investigat...
We show that the universal behavior of the Rouse-mode relaxation in polymer systems-which has been r...
A protein molecule possesses many conformational substates that are likely arranged in . a hierarch...
La thèse décrit la complexité de la dynamique locale des protéines dépliées sur des échelles de temp...
The thesis describes the intricacy of local dynamics of unfolded proteins on ps-ns timescales probed...
We study theoretically the dynamics of living polymers which can add and subtract monomer units at t...
The “protein structure-function” paradigm, which states that proteins adopt nearly rigid 3-dimension...
Features of the renormalized and twice renormalized Rouse models were examined numerically. Based on...
We use molecular dynamics simulations of the Kremer–Grest (KG) bead–spring model of polymer chains o...
Polymeric and biological disordered materials are characterized by unique dynamical features. Althou...
The relaxation behaviour of various statistical and thermodynamic many body systems like percolating...
Intrinsically disordered proteins (IDPs) access highly diverse ensembles of conformations in their f...
Static disorder has recently been implicated in the non-exponential kinetics of the unfolding of sin...
We study theoretically the behaviour of a system of « living polymers » (polymers that can break and...
11 p.Using molecular dynamic simulations we study the quench of a homopolymer chain into a poor solv...
The Langevin dynamics of a self-interacting chain embedded in a quenched random medium is investigat...
We show that the universal behavior of the Rouse-mode relaxation in polymer systems-which has been r...
A protein molecule possesses many conformational substates that are likely arranged in . a hierarch...
La thèse décrit la complexité de la dynamique locale des protéines dépliées sur des échelles de temp...
The thesis describes the intricacy of local dynamics of unfolded proteins on ps-ns timescales probed...
We study theoretically the dynamics of living polymers which can add and subtract monomer units at t...
The “protein structure-function” paradigm, which states that proteins adopt nearly rigid 3-dimension...
Features of the renormalized and twice renormalized Rouse models were examined numerically. Based on...
We use molecular dynamics simulations of the Kremer–Grest (KG) bead–spring model of polymer chains o...