Very-Long-Distance Correlations in Proteins Revealed by Solid-State NMR Spectroscopy

被引：19

作者：

Hu, Bingwen ^{[1
,2
]}

Trebosc, Julien ^{[3
]}

Lafon, Oliver ^{[3
]}

Chen, Qun ^{[1
,2
]}

Masuda, Yuichi ^{[4
]}

Takegoshi, K. ^{[5
]}

Amoureux, Jean-Paul ^{[3
]}

机构：

[1] E China Normal Univ, Dept Phys, Shanghai 200062, Peoples R China

[2] E China Normal Univ, Shanghai Key Lab Magnet Resonance, Shanghai 200062, Peoples R China

[3] Lille N France Univ, UCCS, F-59652 Villeneuve Dascq, France

[4] Tohoku Univ, Grad Sch Pharmaceut Sci, Tokyo 9808578, Japan

[5] Kyoto Univ, Dept Chem, Grad Sch Sci, Kyoto 6068502, Japan

来源：

CHEMPHYSCHEM | 2012年 / 13卷 / 16期

基金：

中国国家自然科学基金;

关键词：

Amyloid beta-peptides; magic-angle spinning; NMR spectroscopy; polarization transfer; protein structures; AMYLOID FIBRILS; 3D STRUCTURE; RESONANCE; DYNAMICS;

D O I：

10.1002/cphc.201200548

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

I still see you: A new pulse sequence, SHA+, little sensitive to dipolar truncation, allows direct or relayed polarization transfer between 13C atoms, distant by 3.5-9.6 Å, in amyloid fibrils (see picture). SHA+ can also be used in a broadband way with the weak rf-condition of v1vR≈0.2-0.3 which permits the investigation of temperature-sensitive biological systems. © 2012 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：3585 / 3588

页数：4

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