Temperature Dependence of Protein Folding Deduced from Quantum Transition
Liaofu Luo, Jun Lu

TL;DR
This paper introduces a quantum theoretical framework for understanding protein folding, explaining temperature effects and non-Arrhenius behavior through quantum transitions, and aligns well with experimental data.
Contribution
It presents a novel quantum transition model for protein folding, providing a natural explanation for temperature dependence and non-Arrhenius behavior.
Findings
The quantum model accurately predicts folding rates across temperatures.
The theory explains non-Arrhenius temperature dependence.
Experimental data aligns with the quantum-based rate formula.
Abstract
A quantum theory on conformation-electron system is presented. Protein folding is regarded as the quantum transition between torsion states on polypeptide chain, and the folding rate is calculated by nonadiabatic operator method. The theory is used to study the temperature dependences of folding rate of 15 proteins and their non-Arrhenius behavior can all be deduced in a natural way. A general formula on the rate-temperature dependence has been deduced which is in good accordance with experimental data. These temperature dependences are further analyzed in terms of torsion potential parameters. Our results show it is necessary to move outside the realm of classical physics when the temperature dependence of protein folding is studied quantitatively.
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Taxonomy
TopicsProtein Structure and Dynamics · Enzyme Structure and Function · RNA and protein synthesis mechanisms
