Adsorption vs. folding of a Hydrophobic Chain Protein Model near an Attractive Surface

TL;DR

This study uses multicanonical Monte Carlo simulations to explore how a coarse-grained hydrophobic protein model behaves near an attractive surface, focusing on the competition between folding and adsorption.

Contribution

It introduces a detailed computational analysis of folding versus adsorption in a simplified protein-surface interaction model using advanced simulation techniques.

Findings

Thermodynamic properties differ significantly between folding and adsorption.

Structural parameters reveal distinct conformational states near the surface.

The Lennard-Jones potential effectively models monomer-surface interactions.

Abstract

The folding vs. adsorption behaviour of a coarse-grained off-lattice protein model near an attractive surface is presented within the frame of a Multicanonical Monte Carlo simulations. In the polymer-surface model, the Lennard-Jones potential is assumed as an interaction potential between the effective monomers and the attractive surface. Thermodynamic properties and some structural parameters for the minimum energy conformations are calculated for comparison of the folding and adsorption cases.