学术探索
学术期刊
新闻热点
数据分析
智能评审

NMR in the SPINE structural proteomics project

被引：13
作者：
Ab, E.
Atkinson, A. R.
Banci, L.
Bertini, I.
Ciofi-Baffoni, S.
Brunner, K.
Diercks, T.
Doetsch, V.
Engelke, F.
Folkers, G. E.
Griesinger, C.
Gronwald, W.
Guenther, U.
Habeck, M.
de Jong, R. N.
Kalbitzer, H. R.
Kieffer, B.
Leeflang, B. R.
Loss, S.
Luchinat, C.
Marquardsen, T.
Moskau, D.
Neidig, K. -P.
Nilges, M.
Piccioli, M.
Pierattelli, R.
Rieping, W.
Schippmann, T.
Schwalbe, H.
Trave, G.
Trenner, J.
Woehnert, J.
Zweckstetter, M.
Kaptein, R.
机构：
[1] Univ Utrecht, Bijvoet Ctr Biomol Res, NL-3584 CH Utrecht, Netherlands
[2] Inst Genet & Biol Mol & Cellulaire, F-67404 Illkirch Graffenstaden, France
[3] Univ Florence, CIRMMP, CERM, I-50019 Sesto Fiorentino, Italy
[4] Univ Regensburg, Dept Biophys & Phys Biochem, D-8400 Regensburg, Germany
[5] Goethe Univ Frankfurt, Ctr Biomol Magnet Resonance, D-6000 Frankfurt, Germany
[6] Bruker Biospin GmbH, Rheinstetten, Germany
[7] Max Planck Inst Biophys Chem, Gottingen, Germany
[8] Inst Pasteur, F-75724 Paris, France
[9] Bruker Biospin AG, Fallanden, Switzerland
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2006年 / 62卷
关键词：
D O I：
10.1107/S0907444906032070
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
This paper describes the developments, role and contributions of the NMR spectroscopy groups in the Structural Proteomics In Europe ( SPINE) consortium. Focusing on the development of high- throughput ( HTP) pipelines for NMR structure determinations of proteins, all aspects from sample preparation, data acquisition, data processing, data analysis to structure determination have been improved with respect to sensitivity, automation, speed, robustness and validation. Specific highlights are protonless C-13-direct detection methods and inferential structure determinations ( ISD). In addition to technological improvements, these methods have been applied to deliver over 60 NMR structures of proteins, among which are five that failed to crystallize. The inclusion of NMR spectroscopy in structural proteomics pipelines improves the success rate for protein structure determinations.
引用
收藏
页码：1150 / 1161
页数：12
相关论文
共 82 条
[1]   Direct use of unassigned resonances in NMR structure calculations with proxy residues [J].
Ab, Eiso ;
Pugh, David J. R. ;
Kaptein, Robert ;
Boelens, Rolf ;
Bonvin, Alexandre M. J. J. .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (23) :7566-7571
[2]   Spin-state selection filters for the measurement of heteronuclear one-bond coupling constants [J].
Andersson, P ;
Weigelt, J ;
Otting, G .
JOURNAL OF BIOMOLECULAR NMR, 1998, 12 (03) :435-441
[3]   A hint to search for metalloproteins in gene banks [J].
Andreini, C ;
Bertini, I ;
Rosato, A .
BIOINFORMATICS, 2004, 20 (09) :1373-1380
[4]   Structural interplay between calcium(II) and copper(II) binding to S100A13 protein [J].
Arnesano, F ;
Banci, L ;
Bertini, I ;
Fantoni, A ;
Tenori, L ;
Viezzoli, MS .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2005, 44 (39) :6341-6344
[5]   Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding [J].
Arnesano, F ;
Balatri, E ;
Banci, L ;
Bertini, I ;
Winge, DR .
STRUCTURE, 2005, 13 (05) :713-722
[6]   Ortholog search of proteins involved in copper delivery to cytochrorne c oxidase and functional analysis of paralogs and gene neighbors by genomic context [J].
Arnesano, F ;
Banci, L ;
Bertini, I ;
Martinelli, M .
JOURNAL OF PROTEOME RESEARCH, 2005, 4 (01) :63-70
[7]   A docking approach to the study of copper trafficking proteins: Interaction between metallochaperones and soluble domains of copper ATPases [J].
Arnesano, F ;
Banci, L ;
Bertini, I ;
Bonvin, AMJJ .
STRUCTURE, 2004, 12 (04) :669-676
[8]   A strategy for the NMR characterization of type II copper(II) proteins:: the case of the copper trafficking protein CopC from Pseudomonas syringae [J].
Arnesano, F ;
Banci, L ;
Bertini, I ;
Felli, IC ;
Luchinat, C ;
Thompsett, AR .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2003, 125 (24) :7200-7208
[9]   A redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites [J].
Arnesano, F ;
Banci, L ;
Bertini, I ;
Mangani, S ;
Thompsett, AR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (07) :3814-3819
[10]   Solution structure of human β-parvalbumin and structural comparison with its paralog α-parvalbumin and with their rat orthologs [J].
Babini, E ;
Bertini, I ;
Capozzi, F ;
Del Bianco, C ;
Hollender, D ;
Kiss, T ;
Luchinat, C ;
Quattrone, A .
BIOCHEMISTRY, 2004, 43 (51) :16076-16085
123456789