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The Molten Globule, and Two-State vs. Non-Two-State Folding of Globular Proteins
Version 1
: Received: 19 February 2020 / Approved: 20 February 2020 / Online: 20 February 2020 (07:12:46 CET)
A peer-reviewed article of this Preprint also exists.
Kuwajima, K. The Molten Globule, and Two-State vs. Non-Two-State Folding of Globular Proteins. Biomolecules 2020, 10, 407. Kuwajima, K. The Molten Globule, and Two-State vs. Non-Two-State Folding of Globular Proteins. Biomolecules 2020, 10, 407.
Abstract
From experimental studies of protein folding, it is now clear that there are two types of folding behavior, i.e., two-state folding and non-two-state folding, and understanding the relationships between these apparently different folding behaviors is essential for fully elucidating the molecular mechanisms of protein folding. This article describes how the presence of the two types of folding behavior has been confirmed experimentally, and discusses the relationships between the two-state and the non-two-state folding reactions, on the basis of available data on the correlations of the folding rate constant with various structure-based properties, which are determined primarily by the backbone topology of proteins. Finally, a two-stage hierarchical model is proposed as a general mechanism of protein folding. In this model, protein folding occurs in a hierarchical manner, reflecting the hierarchy of the native three-dimensional structure, as embodied in the case of non-two-state folding with an accumulation of the molten globule state as a folding intermediate. The two-state folding is thus merely a simplified version of the hierarchical folding caused either by an alteration in the rate-limiting step of folding or by destabilization of the intermediate.
Keywords
protein folding; molten globule state; two-state proteins; non-two-state proteins
Subject
Biology and Life Sciences, Biophysics
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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