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dc.contributor.author | Katayama, Kota | en |
dc.contributor.author | Nonaka, Yuki | en |
dc.contributor.author | Tsutsui, Kei | en |
dc.contributor.author | Imai, Hiroo | en |
dc.contributor.author | Kandori, Hideki | en |
dc.contributor.alternative | 筒井, 圭 | ja |
dc.contributor.alternative | 今井, 啓雄 | ja |
dc.date.accessioned | 2018-02-15T06:53:40Z | - |
dc.date.available | 2018-02-15T06:53:40Z | - |
dc.date.issued | 2017-07-7 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | http://hdl.handle.net/2433/229124 | - |
dc.description.abstract | Protein-bound water molecules are essential for the structure and function of many membrane proteins, including G-protein-coupled receptors (GPCRs). Our prior work focused on studying the primate green- (MG) and red- (MR) sensitive visual pigments using low-temperature Fourier transform infrared (FTIR) spectroscopy, which revealed protein-bound waters in both visual pigments. Although the internal waters are located in the vicinity of both the retinal Schiff base and retinal β-ionone ring, only the latter showed differences between MG and MR, which suggests their role in color tuning. Here, we report FTIR spectra of primate blue-sensitive pigment (MB) in the entire mid-IR region, which reveal the presence of internal waters that possess unique water vibrational signals that are reminiscent of a water cluster. These vibrational signals of the waters are influenced by mutations at position Glu113 and Trp265 in Rh, which suggest that these waters are situated between these two residues. Because Tyr265 is the key residue for achieving the spectral blue-shift in λmax of MB, we propose that these waters are responsible for the increase in polarity toward the retinal Schiff base, which leads to the localization of the positive charge in the Schiff base and consequently causes the blue-shift of λmax. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Springer Nature | en |
dc.rights | © The Author(s) 2017 | en |
dc.rights | This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. | en |
dc.subject | Biophysical chemistry | en |
dc.subject | Molecular biophysics | en |
dc.subject | Photobiology | en |
dc.subject | Structural biology | en |
dc.title | Spectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.jtitle | Scientific reports | en |
dc.identifier.volume | 7 | - |
dc.relation.doi | 10.1038/s41598-017-05177-4 | - |
dc.textversion | publisher | - |
dc.identifier.artnum | 4904 | - |
dc.identifier.pmid | 28687791 | - |
dcterms.accessRights | open access | - |
出現コレクション: | 学術雑誌掲載論文等 |
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