Neutron crystallography of photoactive yellow protein reveals unusual protonation state of Arg52 in the crystal

Because of its high pK(a), arginine (Arg) is believed to be protonated even in the hydrophobic environment of the protein interior. However, our neutron crystallographic structure of photoactive yellow protein, a light sensor, demonstrated that Arg52 adopts an electrically neutral form. We also show...

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Detalles Bibliográficos
Autores principales: Yonezawa, Kento, Shimizu, Nobutaka, Kurihara, Kazuo, Yamazaki, Yoichi, Kamikubo, Hironari, Kataoka, Mikio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5570954/
https://www.ncbi.nlm.nih.gov/pubmed/28839266
http://dx.doi.org/10.1038/s41598-017-09718-9

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5570954/
https://www.ncbi.nlm.nih.gov/pubmed/28839266
http://dx.doi.org/10.1038/s41598-017-09718-9

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