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Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy.

Nature 420 98-102 (2002)
Cited: 296 times
EuropePMC logo PMID: 12422222

Abstract

The determination of a representative set of protein structures is a chief aim in structural genomics. Solid-state NMR may have a crucial role in structural investigations of those proteins that do not easily form crystals or are not accessible to solution NMR, such as amyloid systems or membrane proteins. Here we present a protein structure determined by solid-state magic-angle-spinning (MAS) NMR. Almost complete (13)C and (15)N resonance assignments for a micro-crystalline preparation of the alpha-spectrin Src-homology 3 (SH3) domain formed the basis for the extraction of a set of distance restraints. These restraints were derived from proton-driven spin diffusion (PDSD) spectra of biosynthetically site-directed, labelled samples obtained from bacteria grown using [1,3-(13)C]glycerol or [2-(13)C]glycerol as carbon sources. This allowed the observation of long-range distance correlations up to approximately 7 A. The calculated global fold of the alpha-spectrin SH3 domain is based on 286 inter-residue (13)C-(13)C and six (15)N-(15)N restraints, all self-consistently obtained by solid-state MAS NMR. This MAS NMR procedure should be widely applicable to small membrane proteins that can be expressed in bacteria.

Reviews citing this publication (72)

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  41. Robust NMR approaches for the determination of homonuclear dipole-dipole coupling constants in studies of solid materials and biomolecules. Saalwächter K. Chemphyschem 14 3000-3014 (2013)
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  51. Challenges in numerical simulations of solid-state NMR experiments: spin exchange pulse sequences. Vosegaard T. Solid State Nucl Magn Reson 38 77-83 (2010)
  52. Trends in solid-state NMR spectroscopy and their relevance for bioanalytics. Paasch S, Brunner E. Anal Bioanal Chem 398 2351-2362 (2010)
  53. Indirect detection of nitrogen-14 in solid-state NMR spectroscopy. Cavadini S. Prog Nucl Magn Reson Spectrosc 56 46-77 (2010)
  54. What can solid state NMR contribute to our understanding of protein folding? Hu KN, Tycko R. Biophys. Chem. 151 10-21 (2010)
  55. Prions: En route from structural models to structures. Böckmann A, Meier BH. Prion 4 72-79 (2010)
  56. Genomics and bioinformatics resources for crop improvement. Mochida K, Shinozaki K. Plant Cell Physiol. 51 497-523 (2010)
  57. Membrane binding of lipidated Ras peptides and proteins--the structural point of view. Brunsveld L, Waldmann H, Huster D. Biochim. Biophys. Acta 1788 273-288 (2009)
  58. Recent advances in solid-state NMR spectroscopy of spin I=1/2 nuclei. Lesage A. Phys Chem Chem Phys 11 6876-6891 (2009)
  59. Retinal conformation and dynamics in activation of rhodopsin illuminated by solid-state H NMR spectroscopy. Brown MF, Martínez-Mayorga K, Nakanishi K, Salgado GF, Struts AV. Photochem. Photobiol. 85 442-453 (2009)
  60. Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR. McDermott A. Annu Rev Biophys 38 385-403 (2009)
  61. Solid-state NMR spectroscopy of amyloid proteins. Heise H. Chembiochem 9 179-189 (2008)
  62. Perspectives on NMR in drug discovery: a technique comes of age. Pellecchia M, Bertini I, Cowburn D, Dalvit C, Giralt E, Jahnke W, James TL, Homans SW, Kessler H, Luchinat C, Meyer B, Oschkinat H, Peng J, Schwalbe H, Siegal G. Nat Rev Drug Discov 7 738-745 (2008)
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  64. Structure, dynamics, and assembly of filamentous bacteriophages by nuclear magnetic resonance spectroscopy. Opella SJ, Zeri AC, Park SH. Annu Rev Phys Chem 59 635-657 (2008)
  65. Multidimensional solid state NMR of anisotropic interactions in peptides and proteins. Wylie BJ, Rienstra CM. J Chem Phys 128 052207 (2008)
  66. Magnetic resonance in the solid state: applications to protein folding, amyloid fibrils and membrane proteins. Baldus M. Eur. Biophys. J. 36 Suppl 1 S37-48 (2007)
  67. The structure, dynamics, and energetics of protein adsorption-lessons learned from adsorption of statherin to hydroxyapatite. Goobes G, Goobes R, Shaw WJ, Gibson JM, Long JR, Raghunathan V, Schueler-Furman O, Popham JM, Baker D, Campbell CT, Stayton PS, Drobny GP. Magn Reson Chem 45 Suppl 1 S32-47 (2007)
  68. Investigating transport proteins by solid state NMR. Basting D, Lehner I, Lorch M, Glaubitz C. Naunyn Schmiedebergs Arch. Pharmacol. 372 451-464 (2006)
  69. Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent progress and perspectives. Luca S, Heise H, Lange A, Baldus M. Arch. Pharm. (Weinheim) 338 217-228 (2005)
  70. Structure determination of membrane proteins by NMR spectroscopy. Opella SJ, Marassi FM. Chem. Rev. 104 3587-3606 (2004)
  71. Recent developments in solid-state magic-angle spinning, nuclear magnetic resonance of fully and significantly isotopically labelled peptides and proteins. Straus SK. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 359 997-1008 (2004)
  72. Structural and dynamic studies of proteins by solid-state NMR spectroscopy: rapid movement forward. McDermott AE. Curr. Opin. Struct. Biol. 14 554-561 (2004)

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  1. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH. Science 319 1523-1526 (2008)
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