Directed transport as a mechanism for protein folding in vivo

TL;DR

This paper introduces a Brownian-ratchet model for in vivo protein folding that utilizes energy-driven directed transport in a multidimensional energy landscape, effectively guiding proteins to their native state.

Contribution

It presents a novel model for protein folding based on a Brownian-ratchet mechanism that explains how proteins efficiently fold in vivo without biased transition probabilities.

Findings

Model achieves robust folding from any initial state.

Directed transport overcomes obstacles in the energy landscape.

Solves Levinthal's paradox without biased transitions.

Abstract

We propose a model for protein folding in vivo based on a Brownian-ratchet mechanism in the multidimensional energy landscape space. The device is able to produce directed transport taking advantage of the assumed intrinsic asymmetric properties of the proteins and employing the consumption of energy provided by an external source. Through such a directed transport phenomenon, the polypeptide finds the native state starting from any initial state in the energy landscape with great efficacy and robustness, even in the presence of different type of obstacles. This model solves Levinthal's paradox without requiring biased transition probabilities but at the expense of opening the system to an external field.