# Relaxation kinetics of biological dimer adsorption models

Source: [Relaxation kinetics of biological dimer adsorption models](<https://www.sota2.com/research/paper/68fa202c7a2b558e2932f2ac>)

Collection index: [llms.txt](<https://www.sota2.com/research/llms.txt>)

Data updated: 2025-10-23T21:02:26.782Z

Authors: Andrej Vilfan, Erwin Frey, Franz Schwabl

Published: 2001-08-17T20:21:31.000Z

## Abstract

We discuss the relaxation kinetics of a one-dimensional dimer adsorption model as recently proposed for the binding of biological dimers like kinesin on microtubules. The non-equilibrium dynamics shows several regimes: irreversible adsorption on short time scales, an intermediate plateau followed by a power-law regime and finally exponential relaxation towards equilibrium. In all four regimes we give analytical solutions. The algebraic decay and the scaling behaviour can be explained by mapping onto a simple reaction-diffusion model. We show that there are several possibilities to define the autocorrelation function and that they all asymptotically show exponential decay, however with different time constants. Our findings remain valid if there is an attractive interaction between bound dimers.

## Recorded benchmark results

A research result applies to its stated dataset, split, metric and evaluation configuration. Compare like-for-like settings, preserve the metric's unit and direction, and distinguish paper-reported results from independent reproduction. The best result recorded here is not a claim of exhaustive, current global coverage.

## Original sources and implementation

[Original paper](<https://arxiv.org/abs/cond-mat/0108285>)

[PDF](<https://arxiv.org/pdf/cond-mat/0108285.pdf>)
