The Molten Globule, and Two-State vs. Non-Two-State Folding of Globular Proteins.

Biomolecules
Kunihiro Kuwajima

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 destabiliz...Continue Reading

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Citations

Oct 21, 2020·International Journal of Molecular Sciences·Mateusz BanachIrena Roterman
Mar 7, 2021·International Journal of Molecular Sciences·Aikaterini KefalaMichael Kokkinidis
Apr 22, 2021·Biomacromolecules·Guto G RhysDerek N Woolfson
Apr 21, 2021·Proceedings of the National Academy of Sciences of the United States of America·Rohit JainC Robert Matthews

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Methods Mentioned

BETA
protein folding
circular
NMR
X-ray

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