Chain reconfiguration in active noise

N Samanta, R Chakrabarti - Journal of Physics A: Mathematical …, 2016 - iopscience.iop.org
Journal of Physics A: Mathematical and Theoretical, 2016iopscience.iop.org
In a typical single molecule experiment, the dynamics of an unfolded protein is studied by
determining the reconfiguration time using long-range Förster resonance energy transfer,
where the reconfiguration time is the characteristic decay time of the position correlation
between two residues of the protein. In this paper we theoretically calculate the
reconfiguration time for a single flexible polymer in the presence of active noise. The study
suggests that though the mean square displacement grows faster, the chain reconfiguration …
Abstract
In a typical single molecule experiment, the dynamics of an unfolded protein is studied by determining the reconfiguration time using long-range Förster resonance energy transfer, where the reconfiguration time is the characteristic decay time of the position correlation between two residues of the protein. In this paper we theoretically calculate the reconfiguration time for a single flexible polymer in the presence of active noise. The study suggests that though the mean square displacement grows faster, the chain reconfiguration is always slower in the presence of long-lived active noise with exponential temporal correlation. Similar behavior is observed for a worm-like semi-flexible chain and a Zimm chain. However it is primarily the characteristic correlation time of the active noise and not the strength that controls the increase in the reconfiguration time. In brief, such active noise makes the polymer move faster but the correlation loss between the monomers becomes slow.
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