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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...
| Autores principales: | , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
Nature Publishing Group UK
2017
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| Materias: | |
| 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 |