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Nature and locations of the most slowly exchanging peptide NH protons in residues 1 to 19 of ribonuclease S
https://ir.soken.ac.jp/records/4127
https://ir.soken.ac.jp/records/4127f8bbcc2d-7197-43b0-9e14-2c240543ae38
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||
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| 公開日 | 2013-12-25 | |||||||||
| タイトル | ||||||||||
| タイトル | Nature and locations of the most slowly exchanging peptide NH protons in residues 1 to 19 of ribonuclease S | |||||||||
| タイトル | ||||||||||
| タイトル | Nature and locations of the most slowly exchanging peptide NH protons in residues 1 to 19 of ribonuclease S | |||||||||
| 言語 | en | |||||||||
| 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 |
KUWAJIMA, Kunihiro
× KUWAJIMA, Kunihiro
× BALDWIN, Robert L
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| 著者別名 |
桑島, 邦博
× 桑島, 邦博
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| 抄録 | ||||||||||
| 内容記述タイプ | Abstract | |||||||||
| 内容記述 | The locations have been found of the eight most slowly exchanging peptide protons in residues 1 to 19 of ribonuclease S. The resonance lines of these eight protons are resolved by proton magnetic resonance at 360 MHz when either S-peptide (residues 1 to 19) or peptide 1-15 is bound to S-protein (residues 21 to 124). Other peptide protons have been removed by exchange in the sample preparation ([1H]S-peptide is added to deuterated S-protein in D2O), and also by exchange-out of the less protected protons in residues 1 to 19. At pH 5·1, 0°C, there is a 100-fold difference in rates of exchange between the eight most protected protons and the less protected protons of S-peptide. The highly protected protons are protected 104-fold compared to free S-peptide. The protected protons have been identified by 1H nuclear magnetic resonance after denaturing ribonuclease S in ≥3 m-urea-d4, D2O, pH 2·3, −4°C, followed by comparing the chemical shifts of the remaining eight protons with the known -NH spectrum of the free peptide, which has been assigned from the two-dimensional homonuclear correlated spectrum and by comparison with earlier work. The eight highly protected NH protons are localized in one segment, residues 7 to 14. All eight protons are H-bonded: those of residues 7 to 13 are H-bonded within the 3-13 α-helix and that of residue 14 is H-bonded to the β-sheet. The NH proton of residue 16, which also is H-bonded to the β-sheet, is not one of the highly protected protons. Both the N atoms of the eight NH groups and also the O atoms of their CO acceptor groups are shielded from solvent in most cases, according to the molecular area calculations of Finney (1978). |
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| 書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 169, 号 1, p. 281-297, 発行日 1983-09-05 |
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| 出版者 | ||||||||||
| 出版者 | Elsevier | |||||||||
| ISSN | ||||||||||
| 収録物識別子タイプ | ISSN | |||||||||
| 収録物識別子 | 0022-2836 | |||||||||
| DOI | ||||||||||
| 識別子タイプ | DOI | |||||||||
| 関連識別子 | https://doi.org/10.1016/S0022-2836(83)80184-3 | |||||||||
| 関連名称 | 10.1016/S0022-2836(83)80184-3 | |||||||||
| 権利 | ||||||||||
| 権利情報 | © 1983 Published by Elsevier Ltd. | |||||||||
