Experimental and theoretical study on converting myoglobin into a stable domain-swapped dimer by utilizing a tight hydrogen bond network at the hinge region

Various factors, such as helical propensity and hydrogen bonds, control protein structures. A frequently used model protein, myoglobin (Mb), can perform 3D domain swapping, in which the loop at the hinge region is converted to a helical structure in the dimer. We have previously succeeded in obtaini...

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Detalles Bibliográficos
Autores principales: Xie, Cheng, Shimoyama, Hiromitsu, Yamanaka, Masaru, Nagao, Satoshi, Komori, Hirofumi, Shibata, Naoki, Higuchi, Yoshiki, Shigeta, Yasuteru, Hirota, Shun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2021
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9043842/
https://www.ncbi.nlm.nih.gov/pubmed/35496441
http://dx.doi.org/10.1039/d1ra06888a

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9043842/
https://www.ncbi.nlm.nih.gov/pubmed/35496441
http://dx.doi.org/10.1039/d1ra06888a

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