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  1. 原著論文

Direct Observation of the Protonation States in the Mutant Green Fluorescent Protein

https://repo.qst.go.jp/records/78473
https://repo.qst.go.jp/records/78473
2872f753-4d18-482f-a61a-bd7afc155e79
Item type 学術雑誌論文 / Journal Article(1)
公開日 2019-12-17
タイトル
タイトル Direct Observation of the Protonation States in the Mutant Green Fluorescent Protein
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 Shibazaki, Chie

× Shibazaki, Chie

WEKO 1001184

Shibazaki, Chie

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Shimizu, Rumi

× Shimizu, Rumi

WEKO 1001185

Shimizu, Rumi

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Kagotani, Yuji

× Kagotani, Yuji

WEKO 1001186

Kagotani, Yuji

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Ostermann, Andreas

× Ostermann, Andreas

WEKO 1001187

Ostermann, Andreas

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E. Schrader, Tobias

× E. Schrader, Tobias

WEKO 1001188

E. Schrader, Tobias

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Adachi, Motoyasu

× Adachi, Motoyasu

WEKO 1001189

Adachi, Motoyasu

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Chie, Shibazaki

× Chie, Shibazaki

WEKO 1001190

en Chie, Shibazaki

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Rumi, Shimizu

× Rumi, Shimizu

WEKO 1001191

en Rumi, Shimizu

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Yuji, Kagotani

× Yuji, Kagotani

WEKO 1001192

en Yuji, Kagotani

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Motoyasu, Adachi

× Motoyasu, Adachi

WEKO 1001193

en Motoyasu, Adachi

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抄録
内容記述タイプ Abstract
内容記述 Neutron crystallography has been used to elucidate the protonation states for the enhanced green fluorescent protein, which has revolutionized the imaging technologies. The structure has a deprotonated hydroxyl group in the fluorescent chromophore. Also, the protonation states of His148 and Thr203, as well as the orientation of a critical water molecule in direct contact with the chromophore, could be determined. The results demonstrate that the deprotonated hydroxyl group in the chromophore and the nitrogen atom ND1 in His148 are charged negatively and positively, respectively, forming an ion pair. The position of the two deuterium atoms in the critical water molecule appears to be displaced slightly toward the acceptor oxygen atoms according to their omit maps. This displacement implies the formation of an intriguing electrostatic potential realized inside the protein. Our findings provide new insights into strategy for future protein design with developments for quantum chemical calculations.
書誌情報 The Journal of Physical Chemistry Letters

巻 11, 号 2, p. 492-496, 発行日 2020-01
出版者
出版者 ACS Publications
ISSN
収録物識別子タイプ ISSN
収録物識別子 1948-7185
PubMed番号
識別子タイプ PMID
関連識別子 31880458
DOI
識別子タイプ DOI
関連識別子 10.1021/acs.jpclett.9b03252
関連サイト
識別子タイプ URI
関連識別子 https://pubs.acs.org/doi/10.1021/acs.jpclett.9b03252
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