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  1. 010 学術雑誌論文
  2. 桑島, 邦博 / KUWAJIMA, Kunihiro

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/4127
f8bbcc2d-7197-43b0-9e14-2c240543ae38
Item type 学術雑誌論文 / Journal Article(1)
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

KUWAJIMA, Kunihiro

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BALDWIN, Robert L

× BALDWIN, Robert L

BALDWIN, Robert L

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著者別名 桑島, 邦博

× 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).
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
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.
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