Role of $\alpha$ and $\beta$ relaxations in Collapsing Dynamics of a Polymer Chain in Supercooled Glass-forming Liquid

TL;DR

This study uses computer simulations to reveal that both short-term ($eta$) and long-term ($eta$) relaxations in supercooled liquids significantly influence the stability and collapse dynamics of polymer chains, challenging existing beliefs.

Contribution

It demonstrates through simulations that $eta$ relaxation impacts polymer stability, suggesting a need to revise the vitrification hypothesis in bio-preservation.

Findings

$eta$ relaxation affects polymer collapse dynamics.

Both $eta$ and $eta$ relaxations influence stability.

Results challenge the idea that only $eta$ relaxation controls biomolecular dynamics.

Abstract

Understanding the effect of glassy dynamics on the stability of bio-macromolecules and investigating the underlying relaxation processes governing degradation processes of these macromolecules are of immense importance in the context of bio-preservation. In this work we have studied the stability of a model polymer chain in a supercooled glass-forming liquid at different amount of supercooling in order to understand how dynamics of supercooled liquids influence the collapse behavior of the polymer. Our systematic computer simulation studies find that apart from long time relaxation processes ($\alpha$ relaxation), short time dynamics of the supercooled liquid, known as $\beta$ relaxation plays an important role in controlling the stability of the model polymer. This is in agreement with some recent experimental findings. These observations are in stark contrast with the common belief that only long time relaxation processes are the sole player. We find convincing evidence that suggest that one might need to review the the vitrification hypothesis which postulates that $\alpha$ relaxations control the dynamics of biomolecules and thus $\alpha$-relaxation time should be considered for choosing appropriate bio-preservatives. We hope that our results will lead to understand the primary factors in protein stabilization in the context of bio-preservation.