Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding
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 t...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-05-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/28/9/3970 |
| _version_ | 1827742807796744192 |
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| author | Chiaki Nishimura Takeshi Kikuchi |
| author_facet | Chiaki Nishimura Takeshi Kikuchi |
| author_sort | Chiaki Nishimura |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-11T04:11:35Z |
| format | Article |
| id | doaj.art-d1d9c6da209446f091ab9c1d90d66e37 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-11T04:11:35Z |
| publishDate | 2023-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-d1d9c6da209446f091ab9c1d90d66e372023-11-17T23:25:55ZengMDPI AGMolecules1420-30492023-05-01289397010.3390/molecules28093970Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein MisfoldingChiaki Nishimura0Takeshi Kikuchi1Faculty of Pharmaceutical Sciences, Teikyo Heisei University, Tokyo 164-8530, JapanDepartment of Bioinformatics, College of Life Sciences, Ritsumeikan University, Kusatsu 528-8577, JapanProtein 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.https://www.mdpi.com/1420-3049/28/9/3970apomyoglobinapoleghemoglobinprotein foldingfolding intermediatequench flowhydrophobic buried surface area |
| spellingShingle | Chiaki Nishimura Takeshi Kikuchi Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding Molecules apomyoglobin apoleghemoglobin protein folding folding intermediate quench flow hydrophobic buried surface area |
| title | Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding |
| title_full | Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding |
| title_fullStr | Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding |
| title_full_unstemmed | Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding |
| title_short | Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding |
| title_sort | non native structures of apomyoglobin and apoleghemoglobin in folding intermediates related to the protein misfolding |
| topic | apomyoglobin apoleghemoglobin protein folding folding intermediate quench flow hydrophobic buried surface area |
| url | https://www.mdpi.com/1420-3049/28/9/3970 |
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