Observation of heteronuclear overhauser effects confirms the 15N-1H dipolar relaxation mechanism in a crystalline protein

被引：32

作者：

Giraud, Nicolas

Sein, Julien

Pintacuda, Guido

Bockmann, Anja

Lesage, Anne

Blackledge, Martin

Emsley, Lyndon ^{[1
]}

机构：

[1] Ecole Normale Super Lyon, CNRS, ENS, UMR 5182,Lab Chim, F-69364 Lyon, France

[2] UCBL, CNR, UMR 5086, Inst Biol & Chim Prot, F-69367 Lyon, France

[3] UJF, CEA, CNRS, UMR 5075,Inst Biol Struct Jean Pierre Ebel, F-38027 Grenoble, France

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2006年 / 128卷 / 38期

关键词：

D O I：

10.1021/ja064037g

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The observation of proton to nitrogen-15 heteronuclear Overhauser effects in the microcrystalline protein Crh is used to confirm that the principal mechanism of relaxation of amide nitrogens is due to the fluctuation of the N-H dipolar couplings caused by N-H bond dynamics. Our observations reveal the central role of water as the main source of proton magnetization, and we provide an analysis of the different pathways that could lead to the observed results. Copyright © 2006 American Chemical Society.

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页码：12398 / 12399

页数：2

相关论文

共 15 条

[1] Nuclear overhauser effect (NOE) enhancement of 11B NMR spectra of borane adducts in the solid state [J].

Ashbrook, Sharon E. ;

Dowell, Nicholas G. ;

Prokes, Ivan ;

Wimperis, Stephen .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (21) :6782-6783

[2] Water-protein hydrogen exchange in the micro-crystalline protein Crh as observed by solid state NMR spectroscopy [J].

Böckmann, A ;

Juy, M ;

Bettler, E ;

Emsley, L ;

Galinier, A ;

Penin, F ;

Lesage, A .

JOURNAL OF BIOMOLECULAR NMR, 2005, 32 (03) :195-207

[3] Solid state NMR sequential resonance assignments and conformational analysis of the 2 x 10.4 kDa dimeric form of the Bacillus subtilis protein Crh [J].

Böckmann, A ;

Lange, A ;

Galinier, A ;

Luca, S ;

Giraud, N ;

Juy, M ;

Heise, H ;

Montserret, R ;

Penin, F ;

Baldus, M .

JOURNAL OF BIOMOLECULAR NMR, 2003, 27 (04) :323-339

[4] Direct spectral optimisation of proton-proton homonuclear dipolar decoupling in solid-state NMR [J].

Elena, B ;

de Paëpe, G ;

Emsley, L .

CHEMICAL PHYSICS LETTERS, 2004, 398 (4-6) :532-538

[5] An improved broadband decoupling sequence for liquid crystals and solids [J].

Fung, BM ;

Khitrin, AK ;

Ermolaev, K .

JOURNAL OF MAGNETIC RESONANCE, 2000, 142 (01) :97-101

[6] Quantitative analysis of backbone dynamics in a crystalline protein from nitrogen-15 spin-lattice relaxation [J].

Giraud, N ;

Blackledge, M ;

Goldman, M ;

Böckmann, A ;

Lesage, A ;

Penin, F ;

Emsley, L .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (51) :18190-18201

[7] Cross-relaxation between macromolecular and solvent spins: The role of long-range dipole couplings [J].

Halle, B .

JOURNAL OF CHEMICAL PHYSICS, 2003, 119 (23) :12372-12385

[8] Water-protein interactions in microcrystalline Crh measured by 1H-13C solid-state NMR spectroscopy [J].

Lesage, A ;

Böckmann, A .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2003, 125 (44) :13336-13337

[9] Investigation of dipolar-mediated water-protein interactions in microcrystalline Crh by solid-state NMR spectroscopy [J].

Lesage, Anne ;

Emsley, Lyndon ;

Penin, Francois ;

Bockmann, Anja .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (25) :8246-8255

[10] Review - New tools provide new insights in NMR studies of protein dynamics [J].

Mittermaier, A ;

Kay, LE .

SCIENCE, 2006, 312 (5771) :224-228