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Volumn 253, Issue , 2015, Pages 60-70

NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins

Author keywords

Bioinspired materials; DNP; NMR crystallography; Sample preparation; Sedimentation; Solid State NMR

Indexed keywords

LIGHT POLARIZATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SEDIMENTATION; SILICA;

EID: 84925362330     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2014.12.019     Document Type: Article
Times cited : (21)

References (136)
  • 2
    • 84884217594 scopus 로고    scopus 로고
    • Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue
    • J.-X. Lu, W. Qiang, W.-M. Yau, C.D. Schwieters, S.C. Meredith, and R. Tycko Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue Cell 154 2013 1257 1268 10.1016/j.cell.2013.08.035
    • (2013) Cell , vol.154 , pp. 1257-1268
    • Lu, J.-X.1    Qiang, W.2    Yau, W.-M.3    Schwieters, C.D.4    Meredith, S.C.5    Tycko, R.6
  • 3
    • 84884219396 scopus 로고    scopus 로고
    • Advanced solid-state NMR approaches for structure determination of membrane proteins and amyloid fibrils
    • M. Tang, G. Comellas, and C.M. Rienstra Advanced solid-state NMR approaches for structure determination of membrane proteins and amyloid fibrils Acc. Chem. Res. 46 2013 2080 2088 10.1021/ar4000168
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2080-2088
    • Tang, M.1    Comellas, G.2    Rienstra, C.M.3
  • 4
    • 84884271592 scopus 로고    scopus 로고
    • Structure determination of membrane proteins in their native phospholipid bilayer environment by rotationally aligned solid-state NMR spectroscopy
    • S.J. Opella Structure determination of membrane proteins in their native phospholipid bilayer environment by rotationally aligned solid-state NMR spectroscopy Acc. Chem. Res. 46 2013 2145 2153 10.1021/ar400067z
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2145-2153
    • Opella, S.J.1
  • 5
    • 84884266020 scopus 로고    scopus 로고
    • Solid state NMR strategy for characterizing native membrane protein structures
    • D.T. Murray, N. Das, and T.A. Cross Solid state NMR strategy for characterizing native membrane protein structures Acc. Chem. Res. 46 2013 2172 2181 10.1021/ar3003442
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2172-2181
    • Murray, D.T.1    Das, N.2    Cross, T.A.3
  • 6
    • 84884224184 scopus 로고    scopus 로고
    • Membrane protein structure determination in membrana
    • Y. Ding, Y. Yao, and F.M. Marassi Membrane protein structure determination in membrana Acc. Chem. Res. 46 2013 2182 2190 10.1021/ar400041a
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2182-2190
    • Ding, Y.1    Yao, Y.2    Marassi, F.M.3
  • 7
    • 84882400833 scopus 로고    scopus 로고
    • NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond
    • A. Mainz, T.L. Religa, R. Sprangers, R. Linser, L.E. Kay, and B. Reif NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond Angew. Chem. Int. Ed. 52 2013 8746 8751 10.1002/anie.201301215
    • (2013) Angew. Chem. Int. Ed. , vol.52 , pp. 8746-8751
    • Mainz, A.1    Religa, T.L.2    Sprangers, R.3    Linser, R.4    Kay, L.E.5    Reif, B.6
  • 9
    • 76249111445 scopus 로고    scopus 로고
    • NMR reveals pathway for ferric mineral precursors to the central cavity of ferritin
    • P. Turano, D. Lalli, I.C. Felli, E.C. Theil, and I. Bertini NMR reveals pathway for ferric mineral precursors to the central cavity of ferritin Proc. Natl. Acad. Sci. 107 2010 545 550 10.1073/pnas.0908082106
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 545-550
    • Turano, P.1    Lalli, D.2    Felli, I.C.3    Theil, E.C.4    Bertini, I.5
  • 10
    • 70450189550 scopus 로고    scopus 로고
    • Large protein complexes with extreme rotational correlation times investigated in solution by magic-angle-spinning NMR spectroscopy
    • A. Mainz, S. Jehle, B.J. van Rossum, H. Oschkinat, and B. Reif Large protein complexes with extreme rotational correlation times investigated in solution by magic-angle-spinning NMR spectroscopy J. Am. Chem. Soc. 131 2009 15968 15969
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15968-15969
    • Mainz, A.1    Jehle, S.2    Van Rossum, B.J.3    Oschkinat, H.4    Reif, B.5
  • 11
    • 84910119396 scopus 로고    scopus 로고
    • Immobilization of β-glucuronidase in lysozyme-induced biosilica particles to improve its stability
    • X. Song, Z. Jiang, L. Li, and H. Wu Immobilization of β-glucuronidase in lysozyme-induced biosilica particles to improve its stability Front. Chem. Sci. Eng. 2014 1 9 10.1007/s11705-014-1421-2
    • (2014) Front. Chem. Sci. Eng. , pp. 1-9
    • Song, X.1    Jiang, Z.2    Li, L.3    Wu, H.4
  • 12
    • 84889784915 scopus 로고    scopus 로고
    • SSNMR of biosilica-entrapped enzymes permits an easy assessment of preservation of native conformation in atomic detail
    • M. Fragai, C. Luchinat, T. Martelli, E. Ravera, I. Sagi, and I. Solomonov et al. SSNMR of biosilica-entrapped enzymes permits an easy assessment of preservation of native conformation in atomic detail Chem. Commun. 50 2013 421 423 10.1039/C3CC46896H
    • (2013) Chem. Commun. , vol.50 , pp. 421-423
    • Fragai, M.1    Luchinat, C.2    Martelli, T.3    Ravera, E.4    Sagi, I.5    Solomonov, I.6
  • 13
    • 84884259102 scopus 로고    scopus 로고
    • Solid-state NMR studies of biomineralization peptides and proteins
    • A. Roehrich, and G. Drobny Solid-state NMR studies of biomineralization peptides and proteins Acc. Chem. Res. 46 2013 2136 2144 10.1021/ar300321e
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2136-2144
    • Roehrich, A.1    Drobny, G.2
  • 14
    • 84899978326 scopus 로고    scopus 로고
    • Past and future solid-state NMR spectroscopy studies at the convergence point between biology and materials research
    • G. Goobes Past and future solid-state NMR spectroscopy studies at the convergence point between biology and materials research Isr. J. Chem. 54 2014 113 124 10.1002/ijch.201300113
    • (2014) Isr. J. Chem. , vol.54 , pp. 113-124
    • Goobes, G.1
  • 15
    • 0037361828 scopus 로고    scopus 로고
    • Solid-state 29Si MAS NMR studies of diatoms: structural characterization of biosilica deposits
    • R. Bertermann, N. Kröger, and R. Tacke Solid-state 29Si MAS NMR studies of diatoms: structural characterization of biosilica deposits Anal. Bioanal. Chem. 375 2003 630 634 10.1007/s00216-003-1769-5
    • (2003) Anal. Bioanal. Chem. , vol.375 , pp. 630-634
    • Bertermann, R.1    Kröger, N.2    Tacke, R.3
  • 16
    • 84905017488 scopus 로고    scopus 로고
    • Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature
    • M. Lee, and M. Hong Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature J. Biomol. NMR 59 2014 263 277 10.1007/s10858-014-9845-z
    • (2014) J. Biomol. NMR , vol.59 , pp. 263-277
    • Lee, M.1    Hong, M.2
  • 17
    • 84889803432 scopus 로고    scopus 로고
    • Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins
    • M. Fragai, C. Luchinat, G. Parigi, and E. Ravera Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins J. Biomol. NMR 57 2013 155 166 10.1007/s10858-013-9776-0
    • (2013) J. Biomol. NMR , vol.57 , pp. 155-166
    • Fragai, M.1    Luchinat, C.2    Parigi, G.3    Ravera, E.4
  • 18
    • 84867559987 scopus 로고    scopus 로고
    • Protein linewidth and solvent dynamics in frozen solution NMR
    • A.B. Siemer, K.-Y. Huang, and A.E. McDermott Protein linewidth and solvent dynamics in frozen solution NMR PLoS One 7 2012 e47242
    • (2012) PLoS One , vol.7
    • Siemer, A.B.1    Huang, K.-Y.2    McDermott, A.E.3
  • 19
    • 80755176781 scopus 로고    scopus 로고
    • Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR
    • A.H. Linden, W.T. Franks, Ü. Akbey, S. Lange, B.-J. van Rossum, and H. Oschkinat Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR J. Biomol. NMR 51 2011 283 292
    • (2011) J. Biomol. NMR , vol.51 , pp. 283-292
    • Linden, A.H.1    Franks, W.T.2    Akbey, Ü.3    Lange, S.4    Van Rossum, B.-J.5    Oschkinat, H.6
  • 20
    • 36749105542 scopus 로고
    • Transverse relaxation of dipolar coupled spin systems under rf irradiation: detecting motions in solids
    • W.P. Rothwell, and J.S. Waugh Transverse relaxation of dipolar coupled spin systems under rf irradiation: detecting motions in solids J. Chem. Phys. 74 1981 2721 2732 10.1063/1.441433
    • (1981) J. Chem. Phys. , vol.74 , pp. 2721-2732
    • Rothwell, W.P.1    Waugh, J.S.2
  • 21
    • 0000570050 scopus 로고
    • Slow molecular motion detected in the NMR spectra of rotating solids
    • D. Suwelack, W.P. Rothwell, and J.S. Waugh Slow molecular motion detected in the NMR spectra of rotating solids J. Chem. Phys. 73 1980 2559 2569 10.1063/1.440491
    • (1980) J. Chem. Phys. , vol.73 , pp. 2559-2569
    • Suwelack, D.1    Rothwell, W.P.2    Waugh, J.S.3
  • 22
    • 0021755216 scopus 로고
    • High-resolution nitrogen-15 nuclear magnetic resonance studies of.alpha.-lytic protease in solid state. Direct comparison of enzyme structure in solution and solid states
    • T.H. Huang, W.W. Bachovchin, R.G. Griffin, and C.M. Dobson High-resolution nitrogen-15 nuclear magnetic resonance studies of.alpha.-lytic protease in solid state. Direct comparison of enzyme structure in solution and solid states Biochemistry (Mosc.) 23 1984 5933 5937
    • (1984) Biochemistry (Mosc.) , vol.23 , pp. 5933-5937
    • Huang, T.H.1    Bachovchin, W.W.2    Griffin, R.G.3    Dobson, C.M.4
  • 25
    • 0142011632 scopus 로고    scopus 로고
    • Preparation of protein nanocrystals and their characterization by solid state NMR
    • R.W. Martin, and K.W. Zilm Preparation of protein nanocrystals and their characterization by solid state NMR J. Magn. Reson. 165 2003 162 174 10.1016/S1090-7807(03)00253-2
    • (2003) J. Magn. Reson. , vol.165 , pp. 162-174
    • Martin, R.W.1    Zilm, K.W.2
  • 26
    • 0032175923 scopus 로고    scopus 로고
    • Effects of sample preparation conditions on biomolecular solid-state NMR lineshapes
    • D.L. Jakeman, D.J. Mitchell, W.A.:. Shuttleworth, and J.N.S. Evans Effects of sample preparation conditions on biomolecular solid-state NMR lineshapes J. Biomol. NMR 12 1998 417 421
    • (1998) J. Biomol. NMR , vol.12 , pp. 417-421
    • Jakeman, D.L.1    Mitchell, D.J.2    Shuttleworth, W.A.3    Evans, J.N.S.4
  • 27
    • 0034167578 scopus 로고    scopus 로고
    • Sample optimization and identification of signal patterns of amino acid side chains in 2D RFDR spectra of the α-spectrin SH3 domain
    • J. Pauli, B. van Rossum, H. Förster, H.J.M. de Groot, and H. Oschkinat Sample optimization and identification of signal patterns of amino acid side chains in 2D RFDR spectra of the α-spectrin SH3 domain J. Magn. Reson. 143 2000 411 416 10.1006/jmre.2000.2029
    • (2000) J. Magn. Reson. , vol.143 , pp. 411-416
    • Pauli, J.1    Van Rossum, B.2    Förster, H.3    De Groot, H.J.M.4    Oschkinat, H.5
  • 28
    • 0035795429 scopus 로고    scopus 로고
    • Backbone and side-chain 13C and 15N signal assignments of the α-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla
    • J. Pauli, M. Baldus, B. van Rossum, H. de Groot, and H. Oschkinat Backbone and side-chain 13C and 15N signal assignments of the α-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla ChemBioChem 2 2001 272 281 10.1002/1439-7633(20010401)2:4<272::AID-CBIC272>3.0.CO;2-2
    • (2001) ChemBioChem , vol.2 , pp. 272-281
    • Pauli, J.1    Baldus, M.2    Van Rossum, B.3    De Groot, H.4    Oschkinat, H.5
  • 29
    • 0037038365 scopus 로고    scopus 로고
    • Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
    • F. Castellani, B. van Rossum, A. Diehl, M. Schubert, K. Rehbein, and H. Oschkinat Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy Nature 420 2002 98 102
    • (2002) Nature , vol.420 , pp. 98-102
    • Castellani, F.1    Van Rossum, B.2    Diehl, A.3    Schubert, M.4    Rehbein, K.5    Oschkinat, H.6
  • 30
    • 0141483325 scopus 로고    scopus 로고
    • Determination of solid-state NMR structures of proteins by means of three-dimensional 15N-13C-13C dipolar correlation spectroscopy and chemical shift analysis
    • F. Castellani, B.J. van Rossum, A. Diehl, K. Rehbein, and H. Oschkinat Determination of solid-state NMR structures of proteins by means of three-dimensional 15N-13C-13C dipolar correlation spectroscopy and chemical shift analysis Biochemistry (Mosc.) 42 2003 11476 11483
    • (2003) Biochemistry (Mosc.) , vol.42 , pp. 11476-11483
    • Castellani, F.1    Van Rossum, B.J.2    Diehl, A.3    Rehbein, K.4    Oschkinat, H.5
  • 31
    • 0025301788 scopus 로고
    • Structural effects of hydration: Studies of lysozyme by 13C solids NMR
    • S.D. Kennedy, and R.G. Bryant Structural effects of hydration: Studies of lysozyme by 13C solids NMR Biopolymers 29 1990 1801 1806 10.1002/bip.360291411
    • (1990) Biopolymers , vol.29 , pp. 1801-1806
    • Kennedy, S.D.1    Bryant, R.G.2
  • 32
    • 0027138521 scopus 로고
    • The influence of hydration on the conformation of bovine serum albumin studied by solid-state 13C NMR spectroscopy
    • R.B. Gregory, M. Gangoda, R.K. Gilpin, and W. Su The influence of hydration on the conformation of bovine serum albumin studied by solid-state 13C NMR spectroscopy Biopolymers 33 1993 1871 1876 10.1002/bip.360331212
    • (1993) Biopolymers , vol.33 , pp. 1871-1876
    • Gregory, R.B.1    Gangoda, M.2    Gilpin, R.K.3    Su, W.4
  • 33
    • 24744465473 scopus 로고    scopus 로고
    • High-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin
    • K. Seidel, M. Etzkorn, H. Heise, S. Becker, and M. Baldus High-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin Chembiochem Eur. J. Chem. Biol. 6 2005 1638 1647 10.1002/cbic.200500085
    • (2005) Chembiochem Eur. J. Chem. Biol. , vol.6 , pp. 1638-1647
    • Seidel, K.1    Etzkorn, M.2    Heise, H.3    Becker, S.4    Baldus, M.5
  • 34
    • 84884262060 scopus 로고    scopus 로고
    • SedNMR: on the edge between solution and solid-state NMR
    • I. Bertini, C. Luchinat, G. Parigi, and E. Ravera SedNMR: on the edge between solution and solid-state NMR Acc. Chem. Res. 46 2013 2059 2069 10.1021/ar300342f
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2059-2069
    • Bertini, I.1    Luchinat, C.2    Parigi, G.3    Ravera, E.4
  • 35
    • 69749098389 scopus 로고    scopus 로고
    • Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance
    • K.-N. Hu, R.H. Havlin, W.-M. Yau, and R. Tycko Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance J. Mol. Biol. 392 2009 1055 1073 10.1016/j.jmb.2009.07.073
    • (2009) J. Mol. Biol. , vol.392 , pp. 1055-1073
    • Hu, K.-N.1    Havlin, R.H.2    Yau, W.-M.3    Tycko, R.4
  • 36
    • 14744272629 scopus 로고    scopus 로고
    • Probing site-specific conformational distributions in protein folding with solid-state NMR
    • R.H. Havlin, and R. Tycko Probing site-specific conformational distributions in protein folding with solid-state NMR Proc. Natl. Acad. Sci. U. S. A. 102 2005 3284 3289 10.1073/pnas.0406130102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 3284-3289
    • Havlin, R.H.1    Tycko, R.2
  • 37
    • 55049102570 scopus 로고    scopus 로고
    • Biomolecular solid state NMR with magic-angle spinning at 25 K
    • K.R. Thurber, and R. Tycko Biomolecular solid state NMR with magic-angle spinning at 25 K J. Magn. Reson. 195 2008 179 186
    • (2008) J. Magn. Reson. , vol.195 , pp. 179-186
    • Thurber, K.R.1    Tycko, R.2
  • 38
    • 2842591175 scopus 로고
    • Apparatus for low-temperature magic-angle spinning NMR
    • P.J. Allen, F. Creuzet, H.J.M. De Groot, and R.G. Griffin Apparatus for low-temperature magic-angle spinning NMR J. Magn. Reson. 1969 92 1991 614 617 10.1016/0022-2364(91)90357-Y
    • (1991) J. Magn. Reson. , vol.1969 , Issue.92 , pp. 614-617
    • Allen, P.J.1    Creuzet, F.2    De Groot, H.J.M.3    Griffin, R.G.4
  • 40
    • 84884274067 scopus 로고    scopus 로고
    • NMR at low and ultralow temperatures
    • R. Tycko NMR at low and ultralow temperatures Acc. Chem. Res. 46 2013 1923 1932 10.1021/ar300358z
    • (2013) Acc. Chem. Res. , vol.46 , pp. 1923-1932
    • Tycko, R.1
  • 42
    • 1942489080 scopus 로고    scopus 로고
    • Assignment of the backbone resonances for microcrystalline ubiquitin
    • T.I. Igumenova, A.J. Wand, and A.E. McDermott Assignment of the backbone resonances for microcrystalline ubiquitin J. Am. Chem. Soc. 126 2004 5323 5331
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5323-5331
    • Igumenova, T.I.1    Wand, A.J.2    McDermott, A.E.3
  • 44
    • 0036792145 scopus 로고    scopus 로고
    • The development and application of a method to quantify the quality of cryoprotectant solutions using standard area-detector X-ray images
    • M.B. McFerrin, and E.H. Snell The development and application of a method to quantify the quality of cryoprotectant solutions using standard area-detector X-ray images J. Appl. Crystallogr. 35 2002 538 545 10.1107/S0021889802009238
    • (2002) J. Appl. Crystallogr. , vol.35 , pp. 538-545
    • McFerrin, M.B.1    Snell, E.H.2
  • 50
    • 0003024601 scopus 로고
    • Electron paramagnetic resonance studies in frozen aqueous solutions. Elimination of freezing artifacts
    • J.S. Leigh, and G.H. Reed Electron paramagnetic resonance studies in frozen aqueous solutions. Elimination of freezing artifacts J. Phys. Chem. 75 1971 1202 1204 10.1021/j100679a003
    • (1971) J. Phys. Chem. , vol.75 , pp. 1202-1204
    • Leigh, J.S.1    Reed, G.H.2
  • 51
    • 36849119978 scopus 로고
    • Line shapes of electron paramagnetic resonance signals produced by powders, glasses, and viscous liquids
    • F.K. Kneubühl Line shapes of electron paramagnetic resonance signals produced by powders, glasses, and viscous liquids J. Chem. Phys. 33 1960 1074 1078 10.1063/1.1731336
    • (1960) J. Chem. Phys. , vol.33 , pp. 1074-1078
    • Kneubühl, F.K.1
  • 53
    • 84885534188 scopus 로고    scopus 로고
    • Microcrystalline proteins - an ideal benchmark for methodology development
    • I. Bertini, K.S. McGreevy, G. Parigi, Wiley-VCH Verlag GmbH & Co. KGaA (accessed 18.09.14)
    • W.T. Franks, B.-J. van Rossum, B. Bardiaux, E. Ravera, G. Parigi, and C. Luchinat et al. Microcrystalline proteins - an ideal benchmark for methodology development I. Bertini, K.S. McGreevy, G. Parigi, NMR Biomol. 2012 Wiley-VCH Verlag GmbH & Co. KGaA 376 392 < http://onlinelibrary.wiley.com/doi/10.1002/9783527644506.ch22/summary> (accessed 18.09.14)
    • (2012) NMR Biomol. , pp. 376-392
    • Franks, W.T.1    Van Rossum, B.-J.2    Bardiaux, B.3    Ravera, E.4    Parigi, G.5    Luchinat, C.6
  • 54
    • 84902500094 scopus 로고    scopus 로고
    • Ten years of probabilistic estimates of biocrystal solvent content: new insights via nonparametric kernel density estimate
    • C.X. Weichenberger, and B. Rupp Ten years of probabilistic estimates of biocrystal solvent content: new insights via nonparametric kernel density estimate Acta Crystallogr. D Biol. Crystallogr. 70 2014 1579 1588 10.1107/S1399004714005550
    • (2014) Acta Crystallogr. D Biol. Crystallogr. , vol.70 , pp. 1579-1588
    • Weichenberger, C.X.1    Rupp, B.2
  • 55
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • B.W. Matthews Solvent content of protein crystals J. Mol. Biol. 33 1968 491 497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 56
    • 84893676573 scopus 로고    scopus 로고
    • Strategies for protein cryocrystallography
    • L. Vera, and E.A. Stura Strategies for protein cryocrystallography Cryst. Growth Des. 14 2014 427 435 10.1021/cg301531f
    • (2014) Cryst. Growth Des. , vol.14 , pp. 427-435
    • Vera, L.1    Stura, E.A.2
  • 57
    • 77950828673 scopus 로고    scopus 로고
    • Progress in rational methods of cryoprotection in macromolecular crystallography
    • T. Alcorn, and D.H. Juers Progress in rational methods of cryoprotection in macromolecular crystallography Acta Crystallogr. D Biol. Crystallogr. 66 2010 366 373 10.1107/S090744490903995X
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 366-373
    • Alcorn, T.1    Juers, D.H.2
  • 58
    • 0000449985 scopus 로고    scopus 로고
    • Glycerol concentrations required for cryoprotection of 50 typical protein crystallization solutions
    • E.F. Garman, and E.P. Mitchell Glycerol concentrations required for cryoprotection of 50 typical protein crystallization solutions J. Appl. Crystallogr. 29 1996 584 587 10.1107/S0021889896004190
    • (1996) J. Appl. Crystallogr. , vol.29 , pp. 584-587
    • Garman, E.F.1    Mitchell, E.P.2
  • 59
    • 0002557881 scopus 로고
    • Resolution limits in magic-angle rotation NMR spectra of polycrystalline solids
    • M. Alla, and E. Lippmaa Resolution limits in magic-angle rotation NMR spectra of polycrystalline solids Chem. Phys. Lett. 87 1982 30 33
    • (1982) Chem. Phys. Lett. , vol.87 , pp. 30-33
    • Alla, M.1    Lippmaa, E.2
  • 61
    • 84870847943 scopus 로고    scopus 로고
    • Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals
    • S.A. Shahid, B. Bardiaux, W.T. Franks, L. Krabben, M. Habeck, and B.-J. van Rossum et al. Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals Nat. Methods 9 2012 1212 1217 10.1038/nmeth.2248
    • (2012) Nat. Methods , vol.9 , pp. 1212-1217
    • Shahid, S.A.1    Bardiaux, B.2    Franks, W.T.3    Krabben, L.4    Habeck, M.5    Van Rossum, B.-J.6
  • 62
    • 38349139799 scopus 로고    scopus 로고
    • Crystal polymorphism of protein GB1 examined by solid-state NMR spectroscopy and X-ray diffraction
    • H.L. Frericks Schmidt, L.J. Sperling, Y.G. Gao, B.J. Wylie, J.M. Boettcher, and S.R. Wilson et al. Crystal polymorphism of protein GB1 examined by solid-state NMR spectroscopy and X-ray diffraction J. Phys. Chem. B 111 2007 14362 14369 10.1021/jp075531p
    • (2007) J. Phys. Chem. B , vol.111 , pp. 14362-14369
    • Frericks Schmidt, H.L.1    Sperling, L.J.2    Gao, Y.G.3    Wylie, B.J.4    Boettcher, J.M.5    Wilson, S.R.6
  • 63
    • 84884242342 scopus 로고    scopus 로고
    • Perspectives in enzymology of membrane proteins by solid-state NMR
    • S.J. Ullrich, and C. Glaubitz Perspectives in enzymology of membrane proteins by solid-state NMR Acc. Chem. Res. 46 2013 2164 2171 10.1021/ar4000289
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2164-2171
    • Ullrich, S.J.1    Glaubitz, C.2
  • 64
    • 84899955731 scopus 로고    scopus 로고
    • Recent advances in magic-angle spinning solid-state NMR of proteins
    • V. Ladizhansky Recent advances in magic-angle spinning solid-state NMR of proteins Isr. J. Chem. 54 2014 86 103 10.1002/ijch.201300096
    • (2014) Isr. J. Chem. , vol.54 , pp. 86-103
    • Ladizhansky, V.1
  • 65
    • 84906272789 scopus 로고    scopus 로고
    • Recent advances in magic angle spinning solid state NMR of membrane proteins
    • S. Wang, and V. Ladizhansky Recent advances in magic angle spinning solid state NMR of membrane proteins Prog. Nucl. Magn. Reson. Spectrosc. 82 2014 1 26 10.1016/j.pnmrs.2014.07.001
    • (2014) Prog. Nucl. Magn. Reson. Spectrosc. , vol.82 , pp. 1-26
    • Wang, S.1    Ladizhansky, V.2
  • 66
    • 84899452157 scopus 로고    scopus 로고
    • Detergent optimized membrane protein reconstitution in liposomes for solid state NMR
    • D.T. Murray, J. Griffin, and T.A. Cross Detergent optimized membrane protein reconstitution in liposomes for solid state NMR Biochemistry (Mosc.) 53 2014 2454 2463 10.1021/bi500144h
    • (2014) Biochemistry (Mosc.) , vol.53 , pp. 2454-2463
    • Murray, D.T.1    Griffin, J.2    Cross, T.A.3
  • 67
    • 17444365826 scopus 로고    scopus 로고
    • Bicelles as model membranes for solid- and solution-state NMR studies of membrane peptides and proteins
    • I. Marcotte, and M. Auger Bicelles as model membranes for solid- and solution-state NMR studies of membrane peptides and proteins Concepts Magn. Reson. Part A 24A 2005 17 37 10.1002/cmr.a.20025
    • (2005) Concepts Magn. Reson. Part A , vol.24 A , pp. 17-37
    • Marcotte, I.1    Auger, M.2
  • 68
    • 0021094366 scopus 로고
    • Solid-state nitrogen-15 nuclear magnetic resonance study of the schiff base in bacteriorhodopsin
    • G.S. Harbison, J. Herzfeld, and R.G. Griffin Solid-state nitrogen-15 nuclear magnetic resonance study of the schiff base in bacteriorhodopsin Biochemistry (Mosc.) 22 1983 1 5
    • (1983) Biochemistry (Mosc.) , vol.22 , pp. 1-5
    • Harbison, G.S.1    Herzfeld, J.2    Griffin, R.G.3
  • 69
    • 0021952593 scopus 로고
    • NMR structural analysis of a membrane protein: bacteriorhodopsin peptide backbone orientation and motion
    • B.A. Lewis, G.S. Harbison, J. Herzfeld, and R.G. Griffin NMR structural analysis of a membrane protein: bacteriorhodopsin peptide backbone orientation and motion Biochemistry (Mosc.) 24 1985 4671 4679
    • (1985) Biochemistry (Mosc.) , vol.24 , pp. 4671-4679
    • Lewis, B.A.1    Harbison, G.S.2    Herzfeld, J.3    Griffin, R.G.4
  • 70
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane protein structure and topology
    • F.M. Marassi, and S.J. Opella A solid-state NMR index of helical membrane protein structure and topology J. Magn. Reson. 144 2000 150 155
    • (2000) J. Magn. Reson. , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 72
    • 84865342442 scopus 로고    scopus 로고
    • Magic angle spinning solid-state NMR experiments for structural characterization of proteins
    • V.N. Uversky, A.K. Dunker, Humana Press (accessed 23.09.14)
    • L. Shi, and V. Ladizhansky Magic angle spinning solid-state NMR experiments for structural characterization of proteins V.N. Uversky, A.K. Dunker, Intrinsically Disord. Protein Anal. 2012 Humana Press 153 165 < http://link.springer.com/protocol/10.1007/978-1-61779-927-3-12> (accessed 23.09.14)
    • (2012) Intrinsically Disord. Protein Anal. , pp. 153-165
    • Shi, L.1    Ladizhansky, V.2
  • 74
    • 77955686807 scopus 로고    scopus 로고
    • Effects of proteins on protein diffusion
    • Y. Wang, C. Li, and G.J. Pielak Effects of proteins on protein diffusion J. Am. Chem. Soc. 132 2010 9392 9397 10.1021/ja102296k
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9392-9397
    • Wang, Y.1    Li, C.2    Pielak, G.J.3
  • 76
    • 33744956334 scopus 로고    scopus 로고
    • Intermolecular electrostatic interactions and Brownian tumbling in protein solutions
    • A. Krushelnitsky Intermolecular electrostatic interactions and Brownian tumbling in protein solutions Phys. Chem. Chem. Phys. 8 2006 2117 2128 10.1039/B517448A
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , pp. 2117-2128
    • Krushelnitsky, A.1
  • 77
    • 0019057731 scopus 로고
    • Concentrated protein solutions in the analytical ultracentrifuge
    • S. Lundh Concentrated protein solutions in the analytical ultracentrifuge J. Polym. Sci. Polym. Phys. Ed. 18 1980 1963 1978
    • (1980) J. Polym. Sci. Polym. Phys. Ed. , vol.18 , pp. 1963-1978
    • Lundh, S.1
  • 78
    • 0021836859 scopus 로고
    • Ultacentrifugation of concentrated biopolymer solutions and effect of ascorbate
    • S. Lundh Ultacentrifugation of concentrated biopolymer solutions and effect of ascorbate Arch. Biochem. Biophys. 241 1985 265 274
    • (1985) Arch. Biochem. Biophys. , vol.241 , pp. 265-274
    • Lundh, S.1
  • 79
    • 84884292171 scopus 로고    scopus 로고
    • Water and protein dynamics in sedimented systems: a relaxometric investigation
    • C. Luchinat, G. Parigi, and E. Ravera Water and protein dynamics in sedimented systems: a relaxometric investigation ChemPhysChem 14 2013 3156 3161 10.1002/cphc.201300167
    • (2013) ChemPhysChem , vol.14 , pp. 3156-3161
    • Luchinat, C.1    Parigi, G.2    Ravera, E.3
  • 80
    • 74049116664 scopus 로고    scopus 로고
    • Water and backbone dynamics in a hydrated protein
    • G. Diakova, Y.A. Goddard, J.-P. Korb, and R.G. Bryant Water and backbone dynamics in a hydrated protein Biophys. J. 98 2010 138 146 10.1016/j.bpj.2009.09.054
    • (2010) Biophys. J. , vol.98 , pp. 138-146
    • Diakova, G.1    Goddard, Y.A.2    Korb, J.-P.3    Bryant, R.G.4
  • 81
    • 84875771017 scopus 로고    scopus 로고
    • Experimental determination of microsecond reorientation correlation times in protein solutions
    • E. Ravera, G. Parigi, A. Mainz, T.L. Religa, B. Reif, and C. Luchinat Experimental determination of microsecond reorientation correlation times in protein solutions J. Phys. Chem. B 117 2013 3548 3553 10.1021/jp312561f
    • (2013) J. Phys. Chem. B , vol.117 , pp. 3548-3553
    • Ravera, E.1    Parigi, G.2    Mainz, A.3    Religa, T.L.4    Reif, B.5    Luchinat, C.6
  • 83
    • 0000953276 scopus 로고    scopus 로고
    • 13C-1H dipolar-assisted rotational resonance in magic-angle spinning NMR
    • K. Takegoshi, S. Nakamura, and T. Terao 13C-1H dipolar-assisted rotational resonance in magic-angle spinning NMR Chem. Phys. Lett. 344 2001 631 637 10.1016/S0009-2614(01)00791-6
    • (2001) Chem. Phys. Lett. , vol.344 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 84
    • 34147171102 scopus 로고    scopus 로고
    • Calcium regulates tertiary structure and enzymatic activity of human endometase/matrilysin-2 and its role in promoting human breast cancer cell invasion
    • S. Lee, H.I. Park, and Q.-X.A. Sang Calcium regulates tertiary structure and enzymatic activity of human endometase/matrilysin-2 and its role in promoting human breast cancer cell invasion Biochem. J. 403 2007 31 42 10.1042/BJ20061390
    • (2007) Biochem. J. , vol.403 , pp. 31-42
    • Lee, S.1    Park, H.I.2    Sang, Q.-X.A.3
  • 85
    • 84862998999 scopus 로고    scopus 로고
    • Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II
    • Z. Fisher, C.D. Boone, S.M. Biswas, B. Venkatakrishnan, M. Aggarwal, and C. Tu et al. Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II Protein Eng. Des. Sel. 25 2012 347 355 10.1093/protein/gzs027
    • (2012) Protein Eng. Des. Sel. , vol.25 , pp. 347-355
    • Fisher, Z.1    Boone, C.D.2    Biswas, S.M.3    Venkatakrishnan, B.4    Aggarwal, M.5    Tu, C.6
  • 86
    • 84864675584 scopus 로고    scopus 로고
    • Change in local dynamics of bacteriorhodopsin with retinal isomerization under pressure as studied by fast magic angle spinning NMR
    • I. Kawamura, S. Yamaguchi, H. Nishikawa, K. Tajima, M. Horigome, and S. Tuzi et al. Change in local dynamics of bacteriorhodopsin with retinal isomerization under pressure as studied by fast magic angle spinning NMR Polym. J. 44 2012 863 867 10.1038/pj.2012.116
    • (2012) Polym. J. , vol.44 , pp. 863-867
    • Kawamura, I.1    Yamaguchi, S.2    Nishikawa, H.3    Tajima, K.4    Horigome, M.5    Tuzi, S.6
  • 87
    • 36849106840 scopus 로고
    • Proton enhanced NMR of dilute spins in solids
    • A. Pines, M.G. Gibby, and J.S. Waugh Proton enhanced NMR of dilute spins in solids J. Chem. Phys. 59 1973 569 590
    • (1973) J. Chem. Phys. , vol.59 , pp. 569-590
    • Pines, A.1    Gibby, M.G.2    Waugh, J.S.3
  • 89
    • 84869411125 scopus 로고    scopus 로고
    • Rapid natural-abundance 2D 13C-13C correlation spectroscopy using dynamic nuclear polarization enhanced solid-state NMR and matrix-free sample preparation
    • H. Takahashi, D. Lee, L. Dubois, M. Bardet, S. Hediger, and G. De Paëpe Rapid natural-abundance 2D 13C-13C correlation spectroscopy using dynamic nuclear polarization enhanced solid-state NMR and matrix-free sample preparation Angew. Chem. 124 2012 11936 11939 10.1002/ange.201206102
    • (2012) Angew. Chem. , vol.124 , pp. 11936-11939
    • Takahashi, H.1    Lee, D.2    Dubois, L.3    Bardet, M.4    Hediger, S.5    De Paëpe, G.6
  • 90
    • 84884520064 scopus 로고    scopus 로고
    • Matrix-free dynamic nuclear polarization enables solid-state NMR 13C-13C correlation spectroscopy of proteins at natural isotopic abundance
    • H. Takahashi, S. Hediger, and G. De Paëpe Matrix-free dynamic nuclear polarization enables solid-state NMR 13C-13C correlation spectroscopy of proteins at natural isotopic abundance Chem. Commun. 49 2013 9479 9481
    • (2013) Chem. Commun. , vol.49 , pp. 9479-9481
    • Takahashi, H.1    Hediger, S.2    De Paëpe, G.3
  • 91
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • A.T. Petkova, R.D. Leapman, Z. Guo, W.-M. Yau, M.P. Mattson, and R. Tycko Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils Science 307 2005 262 265 10.1126/science.1105850
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 92
    • 77955273305 scopus 로고    scopus 로고
    • A beta(1-40) forms five distinct amyloid structures whose beta-sheet contents and fibril stabilities are correlated
    • R. Kodali, A.D. Williams, S. Chemuru, and R. Wetzel A beta(1-40) forms five distinct amyloid structures whose beta-sheet contents and fibril stabilities are correlated J. Mol. Biol. 401 2010 503 517
    • (2010) J. Mol. Biol. , vol.401 , pp. 503-517
    • Kodali, R.1    Williams, A.D.2    Chemuru, S.3    Wetzel, R.4
  • 93
    • 79952938717 scopus 로고    scopus 로고
    • The Japanese mutant Aβ (ΔE22-Aβ(1-39)) forms fibrils instantaneously, with low-thioflavin T fluorescence. Seeding of wild-type Aβ(1-40) into atypical fibrils by ΔE22-Aβ(1-39)
    • A.L. Cloe, J.P.R.O. Orgel, J.R. Sachleben, R. Tycko, and S.C. Meredith The Japanese mutant Aβ (ΔE22-Aβ(1-39)) forms fibrils instantaneously, with low-thioflavin T fluorescence. Seeding of wild-type Aβ(1-40) into atypical fibrils by ΔE22-Aβ(1-39) Biochemistry (Mosc.) 50 2011 2026 2039 10.1021/bi1016217
    • (2011) Biochemistry (Mosc.) , vol.50 , pp. 2026-2039
    • Cloe, A.L.1    Orgel, J.P.R.O.2    Sachleben, J.R.3    Tycko, R.4    Meredith, S.C.5
  • 94
    • 79952754330 scopus 로고    scopus 로고
    • Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth
    • W. Qiang, W.-M. Yau, and R. Tycko Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth J. Am. Chem. Soc. 133 2011 4018 4029 10.1021/ja109679q
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 4018-4029
    • Qiang, W.1    Yau, W.-M.2    Tycko, R.3
  • 96
    • 84858663186 scopus 로고    scopus 로고
    • Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils
    • W. Qiang, W.-M. Yau, Y. Luo, M.P. Mattson, and R. Tycko Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils Proc. Natl. Acad. Sci. U. S. A. 109 2012 4443 4448 10.1073/pnas.1111305109
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 4443-4448
    • Qiang, W.1    Yau, W.-M.2    Luo, Y.3    Mattson, M.P.4    Tycko, R.5
  • 97
    • 84877258447 scopus 로고    scopus 로고
    • Polymorph-specific kinetics and thermodynamics of β-amyloid fibril growth
    • W. Qiang, K. Kelley, and R. Tycko Polymorph-specific kinetics and thermodynamics of β-amyloid fibril growth J. Am. Chem. Soc. 135 2013 6860 6871 10.1021/ja311963f
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 6860-6871
    • Qiang, W.1    Kelley, K.2    Tycko, R.3
  • 98
    • 84883449183 scopus 로고    scopus 로고
    • Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-β peptide: perspectives for DNP
    • J.-M.L. del Amo, D. Schneider, A. Loquet, A. Lange, and B. Reif Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-β peptide: perspectives for DNP J. Biomol. NMR 56 2013 359 363 10.1007/s10858-013-9755-5
    • (2013) J. Biomol. NMR , vol.56 , pp. 359-363
    • Del Amo, J.-M.L.1    Schneider, D.2    Loquet, A.3    Lange, A.4    Reif, B.5
  • 99
    • 51249110348 scopus 로고    scopus 로고
    • Bioinspired enzyme encapsulation for biocatalysis
    • L. Betancor, and H.R. Luckarift Bioinspired enzyme encapsulation for biocatalysis Trends Biotechnol. 26 2008 566 572 10.1016/j.tibtech.2008.06.009
    • (2008) Trends Biotechnol. , vol.26 , pp. 566-572
    • Betancor, L.1    Luckarift, H.R.2
  • 100
    • 0037814710 scopus 로고    scopus 로고
    • Polycationic peptides from diatom biosilica that direct silica nanosphere formation
    • N. Kröger, R. Deutzmann, and M. Sumper Polycationic peptides from diatom biosilica that direct silica nanosphere formation Science 286 1999 1129 1132
    • (1999) Science , vol.286 , pp. 1129-1132
    • Kröger, N.1    Deutzmann, R.2    Sumper, M.3
  • 101
    • 33750817561 scopus 로고    scopus 로고
    • Folding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals
    • G. Goobes, R. Goobes, O. Schueler-Furman, D. Baker, P.S. Stayton, and G.P. Drobny Folding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals Proc. Natl. Acad. Sci. 103 2006 16083 16088 10.1073/pnas.0607193103
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 16083-16088
    • Goobes, G.1    Goobes, R.2    Schueler-Furman, O.3    Baker, D.4    Stayton, P.S.5    Drobny, G.P.6
  • 104
    • 29144439731 scopus 로고    scopus 로고
    • Sensitivity considerations in polarization transfer and filtering using dipole-dipole couplings: implications for biomineral systems
    • S.C. Christiansen, N. Hedin, J.D. Epping, M.T. Janicke, Y. del Amo, and M. Demarest et al. Sensitivity considerations in polarization transfer and filtering using dipole-dipole couplings: implications for biomineral systems Solid State Nucl. Magn. Reson. 29 2006 170 182 10.1016/j.ssnmr.2005.10.010
    • (2006) Solid State Nucl. Magn. Reson. , vol.29 , pp. 170-182
    • Christiansen, S.C.1    Hedin, N.2    Epping, J.D.3    Janicke, M.T.4    Del Amo, Y.5    Demarest, M.6
  • 105
    • 41749096800 scopus 로고    scopus 로고
    • The structure and dynamics of poly(l-lysine) in templated silica nanocomposites
    • P.A. Mirau, J.L. Serres, and M. Lyons The structure and dynamics of poly(l-lysine) in templated silica nanocomposites Chem. Mater. 20 2008 2218 2223 10.1021/cm702283u
    • (2008) Chem. Mater. , vol.20 , pp. 2218-2223
    • Mirau, P.A.1    Serres, J.L.2    Lyons, M.3
  • 107
    • 84884228039 scopus 로고    scopus 로고
    • Sensitivity and resolution enhanced solid-state NMR for paramagnetic systems and biomolecules under very fast magic angle spinning
    • S. Parthasarathy, Y. Nishiyama, and Y. Ishii Sensitivity and resolution enhanced solid-state NMR for paramagnetic systems and biomolecules under very fast magic angle spinning Acc. Chem. Res. 46 2013 2127 2135 10.1021/ar4000482
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2127-2135
    • Parthasarathy, S.1    Nishiyama, Y.2    Ishii, Y.3
  • 108
    • 84895081859 scopus 로고    scopus 로고
    • Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd3+-complexes for solid-state NMR spectroscopy
    • S.J. Ullrich, S. Hölper, and C. Glaubitz Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd3+-complexes for solid-state NMR spectroscopy J. Biomol. NMR 58 2014 27 35 10.1007/s10858-013-9800-4
    • (2014) J. Biomol. NMR , vol.58 , pp. 27-35
    • Ullrich, S.J.1    Hölper, S.2    Glaubitz, C.3
  • 109
    • 79960710930 scopus 로고    scopus 로고
    • Solid-state NMR of a large membrane protein by paramagnetic relaxation enhancement
    • M. Tang, D.A. Berthold, and C.M. Rienstra Solid-state NMR of a large membrane protein by paramagnetic relaxation enhancement J. Phys. Chem. Lett. 2 2011 1836 1841 10.1021/jz200768r
    • (2011) J. Phys. Chem. Lett. , vol.2 , pp. 1836-1841
    • Tang, M.1    Berthold, D.A.2    Rienstra, C.M.3
  • 110
    • 84870039330 scopus 로고    scopus 로고
    • A timesaving strategy for MAS NMR spectroscopy by combining non-uniform sampling and paramagnetic relaxation assisted condensed data collection
    • S. Sun, S. Yan, C. Guo, M. Li, J.C. Hoch, and J.C. Williams et al. A timesaving strategy for MAS NMR spectroscopy by combining non-uniform sampling and paramagnetic relaxation assisted condensed data collection J. Phys. Chem. B 116 2012 13585 13596 10.1021/jp3005794
    • (2012) J. Phys. Chem. B , vol.116 , pp. 13585-13596
    • Sun, S.1    Yan, S.2    Guo, C.3    Li, M.4    Hoch, J.C.5    Williams, J.C.6
  • 111
    • 67650534960 scopus 로고    scopus 로고
    • Paramagnetic ions enable tuning of nuclear relaxation rates and provide long-range structural restraints in solid-state NMR of proteins
    • P.S. Nadaud, J.J. Helmus, S.L. Kall, and C.P. Jaroniec Paramagnetic ions enable tuning of nuclear relaxation rates and provide long-range structural restraints in solid-state NMR of proteins J. Am. Chem. Soc. 131 2009 8108 8120 10.1021/ja900224z
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8108-8120
    • Nadaud, P.S.1    Helmus, J.J.2    Kall, S.L.3    Jaroniec, C.P.4
  • 112
    • 84858671526 scopus 로고    scopus 로고
    • Solid state NMR crystallography through paramagnetic restraints
    • C. Luchinat, G. Parigi, E. Ravera, and M. Rinaldelli Solid state NMR crystallography through paramagnetic restraints J. Am. Chem. Soc. 134 2012 5006 5009
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 5006-5009
    • Luchinat, C.1    Parigi, G.2    Ravera, E.3    Rinaldelli, M.4
  • 113
    • 84866409928 scopus 로고    scopus 로고
    • Rapid measurement of pseudocontact shifts in metalloproteins by proton-detected solid-state NMR spectroscopy
    • M.J. Knight, I.C. Felli, R. Pierattelli, I. Bertini, L. Emsley, and T. Herrmann et al. Rapid measurement of pseudocontact shifts in metalloproteins by proton-detected solid-state NMR spectroscopy J. Am. Chem. Soc. 134 2012 14730 14733 10.1021/ja306813j
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 14730-14733
    • Knight, M.J.1    Felli, I.C.2    Pierattelli, R.3    Bertini, I.4    Emsley, L.5    Herrmann, T.6
  • 115
    • 33847634701 scopus 로고    scopus 로고
    • Paramagnetic ions provide precious structural restraints in solid-state NMR of proteins
    • S. Balayssac, I. Bertini, M. Lelli, C. Luchinat, M. Maletta, and K.J. Yeo Paramagnetic ions provide precious structural restraints in solid-state NMR of proteins J. Am. Chem. Soc. 129 2007 2218 2219
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 2218-2219
    • Balayssac, S.1    Bertini, I.2    Lelli, M.3    Luchinat, C.4    Maletta, M.5    Yeo, K.J.6
  • 116
    • 84884248493 scopus 로고    scopus 로고
    • Protein structure determination with paramagnetic solid-state NMR spectroscopy
    • I. Sengupta, P.S. Nadaud, and C.P. Jaroniec Protein structure determination with paramagnetic solid-state NMR spectroscopy Acc. Chem. Res. 46 2013 2117 2126 10.1021/ar300360q
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2117-2126
    • Sengupta, I.1    Nadaud, P.S.2    Jaroniec, C.P.3
  • 119
    • 82455175683 scopus 로고    scopus 로고
    • Fast resonance assignment and fold determination of human superoxide dismutase by high-resolution proton-detected solid state MAS NMR spectroscopy
    • M.J. Knight, A.L. Webber, A.J. Pell, P. Guerry, E. Barbet-Massin, and I. Bertini et al. Fast resonance assignment and fold determination of human superoxide dismutase by high-resolution proton-detected solid state MAS NMR spectroscopy Angew. Chem. Int. Ed. 50 2011 11697 11701
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 11697-11701
    • Knight, M.J.1    Webber, A.L.2    Pell, A.J.3    Guerry, P.4    Barbet-Massin, E.5    Bertini, I.6
  • 120
    • 84861364500 scopus 로고    scopus 로고
    • Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel
    • Y. Su, F. Hu, and M. Hong Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel J. Am. Chem. Soc. 134 2012 8693 8702 10.1021/ja3026328
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 8693-8702
    • Su, Y.1    Hu, F.2    Hong, M.3
  • 122
    • 36448979953 scopus 로고    scopus 로고
    • Absence of Curie relaxation in paramagnetic solids yields long $^1H$ coherence lifetimes
    • G. Kervern, S. Steuernagel, F. Engelke, G. Pintacuda, and L. Emsley Absence of Curie relaxation in paramagnetic solids yields long $^1H$ coherence lifetimes J. Am. Chem. Soc. 129 2007 14118 14119
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14118-14119
    • Kervern, G.1    Steuernagel, S.2    Engelke, F.3    Pintacuda, G.4    Emsley, L.5
  • 123
    • 84885579647 scopus 로고    scopus 로고
    • NMR crystallography on paramagnetic systems: solved and open issues
    • A. Bhaumik, C. Luchinat, G. Parigi, E. Ravera, and M. Rinaldelli NMR crystallography on paramagnetic systems: solved and open issues CrystEngComm 15 2013 8639 8656 10.1039/C3CE41485J
    • (2013) CrystEngComm , vol.15 , pp. 8639-8656
    • Bhaumik, A.1    Luchinat, C.2    Parigi, G.3    Ravera, E.4    Rinaldelli, M.5
  • 124
    • 0000368822 scopus 로고    scopus 로고
    • Cross polarization in the tilted frame: assignment and spectral simplification in heteronuclear spin systems
    • M. Baldus, A.T. Petkova, J. Herzfeld, and R.G. Griffin Cross polarization in the tilted frame: assignment and spectral simplification in heteronuclear spin systems Mol. Phys. 95 1998 1197 1207
    • (1998) Mol. Phys. , vol.95 , pp. 1197-1207
    • Baldus, M.1    Petkova, A.T.2    Herzfeld, J.3    Griffin, R.G.4
  • 125
    • 0018977856 scopus 로고
    • Interpretation of the Mössbauer spectra of the high-potential iron protein from chromatium
    • P. Middleton, D.P.E. Dickson, C.E. Johnson, and J.D. Rush Interpretation of the Mössbauer spectra of the high-potential iron protein from chromatium Eur. J. Biochem. 104 1980 289 296 10.1111/j.1432-1033.1980.tb04427.x
    • (1980) Eur. J. Biochem. , vol.104 , pp. 289-296
    • Middleton, P.1    Dickson, D.P.E.2    Johnson, C.E.3    Rush, J.D.4
  • 126
    • 0001834683 scopus 로고
    • The electronic structure of FeS centers in proteins and models. A contribution to the understanding of their electron transfer properties.
    • I. Bertini, S. Ciurli, and C. Luchinat The electronic structure of FeS centers in proteins and models. A contribution to the understanding of their electron transfer properties. Struct. Bond. 83 1995 1 54
    • (1995) Struct. Bond. , vol.83 , pp. 1-54
    • Bertini, I.1    Ciurli, S.2    Luchinat, C.3
  • 127
    • 0027527387 scopus 로고
    • A Mössbauer investigation of oxidized Fe-4-S-4- HiPIP II from Ectothiorhodospira halophila
    • I. Bertini, A.P. Campos, C. Luchinat, and M. Teixeira A Mössbauer investigation of oxidized Fe-4-S-4- HiPIP II from Ectothiorhodospira halophila J. Inorg. Biochem. 52 1993 227 234
    • (1993) J. Inorg. Biochem. , vol.52 , pp. 227-234
    • Bertini, I.1    Campos, A.P.2    Luchinat, C.3    Teixeira, M.4
  • 129
    • 84855654538 scopus 로고    scopus 로고
    • A comparison of NCO and NCA transfer methods for biological solid-state NMR spectroscopy
    • N.M. Loening, M. Bjerring, N.C. Nielsen, and H. Oschkinat A comparison of NCO and NCA transfer methods for biological solid-state NMR spectroscopy J. Magn. Reson. 214 2012 81 90
    • (2012) J. Magn. Reson. , vol.214 , pp. 81-90
    • Loening, N.M.1    Bjerring, M.2    Nielsen, N.C.3    Oschkinat, H.4
  • 130
    • 77952561316 scopus 로고    scopus 로고
    • Ultrafast MAS solid-state NMR permits extensive 13C and 1H detection in paramagnetic metalloproteins
    • I. Bertini, L. Emsley, M. Lelli, C. Luchinat, J. Mao, and G. Pintacuda Ultrafast MAS solid-state NMR permits extensive 13C and 1H detection in paramagnetic metalloproteins J. Am. Chem. Soc. 132 2010 5558 5559 10.1021/ja100398q
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5558-5559
    • Bertini, I.1    Emsley, L.2    Lelli, M.3    Luchinat, C.4    Mao, J.5    Pintacuda, G.6
  • 131
    • 56249135967 scopus 로고    scopus 로고
    • Paramagnetic shifts in solid-state NMR of proteins to elicit structural information
    • S. Balayssac, I. Bertini, A. Bhaumik, M. Lelli, and C. Luchinat Paramagnetic shifts in solid-state NMR of proteins to elicit structural information Proc. Natl. Acad. Sci. 105 2008 17284 17289 10.1073/pnas.0708460105
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 17284-17289
    • Balayssac, S.1    Bertini, I.2    Bhaumik, A.3    Lelli, M.4    Luchinat, C.5
  • 132
    • 84878639330 scopus 로고    scopus 로고
    • Magic angle spinning NMR structure determination of proteins from pseudocontact shifts
    • J. Li, K.B. Pilla, Q. Li, Z. Zhang, X. Su, and T. Huber et al. Magic angle spinning NMR structure determination of proteins from pseudocontact shifts J. Am. Chem. Soc. 135 2013 8294 8303 10.1021/ja4021149
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 8294-8303
    • Li, J.1    Pilla, K.B.2    Li, Q.3    Zhang, Z.4    Su, X.5    Huber, T.6
  • 133
    • 48749105838 scopus 로고    scopus 로고
    • Prospects for lanthanides in structural biology by NMR
    • G. Otting Prospects for lanthanides in structural biology by NMR J. Biomol. NMR 42 2008 1 9 10.1007/s10858-008-9256-0
    • (2008) J. Biomol. NMR , vol.42 , pp. 1-9
    • Otting, G.1
  • 134
    • 84857003154 scopus 로고    scopus 로고
    • Magnetic anisotropy in a dysprosium/DOTA single-molecule magnet: beyond simple magneto-structural correlations
    • G. Cucinotta, M. Perfetti, J. Luzon, M. Etienne, P.-E. Car, and A. Caneschi et al. Magnetic anisotropy in a dysprosium/DOTA single-molecule magnet: beyond simple magneto-structural correlations Angew. Chem. Int. Ed. 51 2012 1606 1610 10.1002/anie.201107453
    • (2012) Angew. Chem. Int. Ed. , vol.51 , pp. 1606-1610
    • Cucinotta, G.1    Perfetti, M.2    Luzon, J.3    Etienne, M.4    Car, P.-E.5    Caneschi, A.6
  • 135
    • 84939979655 scopus 로고    scopus 로고
    • Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation
    • in press
    • Ding, Fujimoto, Yao, Marassi, Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation, J. Biomol. NMR, in press, http://dx.doi.org/10.1007/s10858-014-9893-4.
    • J. Biomol. NMR
    • Fujimoto, D.1    Marassi, Y.2
  • 136
    • 84920997172 scopus 로고    scopus 로고
    • NMR-detected Brownian dynamics of αB-crystallin over a wide range of concentrations
    • Roos, Link, Balbach, Krushelnitsky, and Saalwachter NMR-detected Brownian dynamics of αB-crystallin over a wide range of concentrations Biophys. J. 108 1 2015 98 106 10.1016/j.bpj.2014.11.1858
    • (2015) Biophys. J. , vol.108 , Issue.1 , pp. 98-106
    • Roos1    Link2    Balbach3    Krushelnitsky4    Saalwachter5


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