Protein Folding as a Quantum Transition Between Conformational States

TL;DR

This paper models protein folding as a quantum conformational transition, deriving folding rates and time-scales from quantum mechanical principles, offering new insights into the folding mechanism.

Contribution

It introduces a quantum theoretical framework for protein folding, linking conformational transitions to quantum states and calculating folding rates based on quantum dynamics.

Findings

Folding time-scale estimated in microseconds to milliseconds.

Transition rate depends on torsion angles and inertial moments.

Temperature dependence of folding rate differs from chemical reactions.

Abstract

The importance of torsion vibration in the transmission of life information is indicated. The localization of quantum torsion state is proved. Following these analyses a formalism on the quantum theory of conformation-electron system is proposed. The conformational-electronic transition is calculated by non-adiabatic operator method. The protein folding is viewed from conformational quantum transition and the folding rate is calculated. The time-scale of microsecond to millisecond for the fundamental folding event (nucleation, collapse, etc) is deduced. The dependence of transition rate W on N inertial moments is given. It indicates how W increases with the number N of torsion angles and decreases with the inertial moment I of atomic group in cooperative transition. The temperature dependence is also deduced which is different from chemical reaction in high-temperature region. It is demonstrated that the conformational dynamics gives deep insights into the folding mechanism and provides a useful tool for analyzing and explaining experimental facts on the rate of protein folding.