Analysis of Two-State Folding Using Parabolic Approximation II: Temperature-Dependence

TL;DR

This paper derives equations describing how temperature affects folding and unfolding kinetics and thermodynamics in two-state protein systems, emphasizing the physical limits of two-state models.

Contribution

It introduces a harmonic Gibbs energy well approach to model temperature dependence in two-state protein folding systems, highlighting the temperature range validity.

Findings

Derived equations for temperature-dependent rate constants and thermodynamic parameters.

Introduced the concept that two-state systems are only physically defined within specific temperature ranges.

Discussed implications for understanding protein folding mechanisms.

Abstract

Equations that govern the temperature-dependence of the rate constants, Gibbs energies,enthalpies, entropies and heat capacities of activation for folding and unfolding of spontaneously-folding fixed two-state systems have been derived using a procedure that treats the denatured and the native conformers as being confined to harmonic Gibbs energy wells. The notion that a two-state system is physically defined only for a set temperature range is introduced. The implications of this novel treatment for protein folding are discussed.