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Updated: Jul 30, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

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Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding

Chiaki Nishimura1, Takeshi Kikuchi2

  • 1Faculty of Pharmaceutical Sciences, Teikyo Heisei University, Tokyo 164-8530, Japan.

Molecules (Basel, Switzerland)
|May 13, 2023
PubMed

Protein folding is essential for a polypeptide chain to acquire its proper structure and function. Globins are a superfamily of ubiquitous heme-binding α-helical proteins whose function is principally to regulate oxygen homoeostasis. In this review, we explore the hierarchical helical formation in the globin proteins apomyoglobin and leghemoglobin, and we discuss the existence of non-native and misfolded structures occurring during the course of folding to its native state. This review summarizes the research aimed at characterizing and comparing the equilibrium and kinetic intermediates, as well as delineating the complete folding pathway at a molecular level, in order to answer the following questions: "What is the mechanism of misfolding via a folding intermediate? Does the non-native structure stabilize the contemporary intermediate structure? Does the non-native structure induce slower folding?" The role of the non-native structures in the folding intermediate related to misfolding is also discussed.

Keywords:
apoleghemoglobinapomyoglobinfolding intermediatehydrophobic buried surface areaprotein foldingquench flow

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