| アイテムタイプ |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2024-12-19 |
| タイトル |
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|
タイトル |
Description of peptide bond planarity from high-resolution neutron crystallography |
|
言語 |
en |
| 言語 |
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|
言語 |
eng |
| 資源タイプ |
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|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| 著者 |
Hanazono Yuya
Hirano Yuu
Tamada Taro
Miki Kunio
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| 抄録 |
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内容記述タイプ |
Abstract |
|
内容記述 |
Neutron crystallography is a highly effective method for visualizing hydrogen atoms in proteins. In our recent study, we successfully determined the high-resolution (1.2 Å) neutron structure of high-potential iron-sulfur protein, refining the coordinates of some amide protons without any geometric restraints. Interestingly, we observed that amide protons are deviated from the peptide plane due to electrostatic interactions. Moreover, the difference in the position of the amide proton of Cys75 between reduced and oxidized states is possibly attributed to the electron storage capacity of the iron-sulfur cluster. Additionally, we have discussed about the rigidity of the iron-sulfur cluster based on the results of the hydrogen-deuterium exchange. Our research underscores the significance of neutron crystallography in protein structure elucidation, enriching our understanding of protein functions at an atomic resolution. |
| 書誌情報 |
Biophysics and Physicobiology
巻 20,
p. e200035,
発行日 2023-09
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| 出版者 |
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出版者 |
一般社団法人 日本生物物理学会 |
| ISSN |
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収録物識別子タイプ |
ISSN |
|
収録物識別子 |
2189-4779 |
| DOI |
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|
識別子タイプ |
DOI |
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関連識別子 |
10.2142/biophysico.bppb-v20.0035 |
