Ordered‐domain unfolding of thermophilic isolated β subunit ATP synthase

The flexibility of the ATP synthase's β subunit promotes its role in the ATP synthase rotational mechanism, but its domains stability remains unknown. A reversible thermal unfolding of the isolated β subunit (Tβ) of the ATP synthase from Bacillus thermophilus PS3, tracked through circular dichr...

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Detalles Bibliográficos
Autores principales: López‐Pérez, Edgar, de Gómez‐Puyou, Marietta Tuena, Nuñez, Concepción José, Zapién, Denise Martínez, Guardado, Salomón Alas, Beltrán, Hiram Isaac, Pérez‐Hernández, Gerardo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2023
Materias:
Full‐length Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10273367/
https://www.ncbi.nlm.nih.gov/pubmed/37252686
http://dx.doi.org/10.1002/pro.4689

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10273367/
https://www.ncbi.nlm.nih.gov/pubmed/37252686
http://dx.doi.org/10.1002/pro.4689

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