메뉴 건너뛰기




Volumn 52, Issue 4, 2012, Pages 283-288

Simultaneous acquisition of PAR and PAIN spectra

Author keywords

CP MAS; PAIN; PAR; Solid state NMR

Indexed keywords

UBIQUITIN;

EID: 84863109575     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-012-9616-7     Document Type: Article
Times cited : (24)

References (40)
  • 3
    • 51649098555 scopus 로고    scopus 로고
    • 3D protein structures by solid-state NMR spectroscopy: Ready for high resolution
    • Böckmann A (2008) 3D protein structures by solid-state NMR spectroscopy: ready for high resolution. Angew Chem Int Ed Engl 47(33):6110-6113
    • (2008) Angew Chem Int Ed Engl , vol.47 , Issue.33 , pp. 6110-6113
    • Böckmann, A.1
  • 5
    • 76249125649 scopus 로고    scopus 로고
    • Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers
    • Cady SD, Schmidt-Rohr K, Wang J, Soto CS, Degrado WF, Hong M (2010) Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers. Nature 463(7281):689-692
    • (2010) Nature , vol.463 , Issue.7281 , pp. 689-692
    • Cady, S.D.1    Schmidt-Rohr, K.2    Wang, J.3    Soto, C.S.4    Degrado, W.F.5    Hong, M.6
  • 6
    • 0037038365 scopus 로고    scopus 로고
    • Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
    • DOI 10.1038/nature01070
    • Castellani F, van Rossum B, Diehl A, Schubert M, Rehbein K, Oschkinat H (2002) Structure of a protein determined by solidstate magic-angle- spinning NMR spectroscopy. Nature 420(6911):98-102 (Pubitemid 35291447)
    • (2002) Nature , vol.420 , Issue.6911 , pp. 98-102
    • Castellani, F.1    Van Rossum, B.2    Diehl, A.3    Schubert, M.4    Rehbein, K.5    Oschklnat, H.6
  • 11
    • 78651277034 scopus 로고    scopus 로고
    • GFT projection NMR spectroscopy for proteins in the solid state
    • Franks WT, Atreya HS, Szyperski T, Rienstra CM (2010) GFT projection NMR spectroscopy for proteins in the solid state. J Biomol NMR 48(4):213-223
    • (2010) J Biomol NMR , vol.48 , Issue.4 , pp. 213-223
    • Franks, W.T.1    Atreya, H.S.2    Szyperski, T.3    Rienstra, C.M.4
  • 13
    • 33746879604 scopus 로고    scopus 로고
    • Distance information from proton-driven spin diffusion under MAS
    • DOI 10.1016/j.cplett.2006.07.005, PII S0009261406009833
    • Grommek A, Meier BH, Ernst M (2006) Distance information from proton-driven spin diffusion under MAS. Chem Phys Lett 427(4-6):404-409 (Pubitemid 44189332)
    • (2006) Chemical Physics Letters , vol.427 , Issue.4-6 , pp. 404-409
    • Grommek, A.1    Meier, B.H.2    Ernst, M.3
  • 15
    • 0000014095 scopus 로고
    • Adiabatic passage Hartmann- Hahn cross polarization in NMR under magic angle sample spinning
    • Hediger S, Meier BH, Ernst RR (1995) Adiabatic passage Hartmann- Hahn cross polarization in NMR under magic angle sample spinning. Chem Phys Lett 240(1):449-456
    • (1995) Chem Phys Lett , vol.240 , Issue.1 , pp. 449-456
    • Hediger, S.1    Meier, B.H.2    Ernst, R.R.3
  • 17
    • 68349098894 scopus 로고    scopus 로고
    • Assigning large proteins in the solid state: A MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins
    • Higman VA, Flinders J, Hiller M, Jehle S, Markovic S, Fiedler S, van Rossum B-J, Oschkinat H (2009) Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins. J Biomol NMR 44(4):245-260
    • (2009) J Biomol NMR , vol.44 , Issue.4 , pp. 245-260
    • Higman, V.A.1    Flinders, J.2    Hiller, M.3    Jehle, S.4    Markovic, S.5    Fiedler, S.6    Van Rossum, B.-J.7    Oschkinat, H.8
  • 22
    • 17044380266 scopus 로고    scopus 로고
    • A concept for rapid protein-structure determination by solid-state NMR spectroscopy
    • Lange A, Becker S, Seidel K, Giller K, Pongs O, Baldus M (2005) A concept for rapid protein-structure determination by solid-state NMR spectroscopy. Angew Chem Int Edit 44(14):2089-2092
    • (2005) Angew Chem Int Edit , vol.44 , Issue.14 , pp. 2089-2092
    • Lange, A.1    Becker, S.2    Seidel, K.3    Giller, K.4    Pongs, O.5    Baldus, M.6
  • 26
    • 79954486030 scopus 로고    scopus 로고
    • Structure calculation from unambiguous long-range amide and methyl 1Hâ '1H distance restraints for a microcrystalline protein with MAS solid-state NMR spectroscopy
    • Linser R, Bardiaux B, Higman V, Fink U, Reif B (2011) Structure calculation from unambiguous long-range amide and methyl 1Hâ '1H distance restraints for a microcrystalline protein with MAS solid-state NMR spectroscopy. J Am Chem Soc 133(15):5905-5912
    • (2011) J Am Chem Soc , vol.133 , Issue.15 , pp. 5905-5912
    • Linser, R.1    Bardiaux, B.2    Higman, V.3    Fink, U.4    Reif, B.5
  • 28
    • 33745855891 scopus 로고    scopus 로고
    • Membrane-bound dimer structure of a β-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMR
    • DOI 10.1021/bi060305b
    • Mani R, Tang M, Wu X, Buffy JJ, Waring AJ, Sherman MA, Hong M (2006) Membrane-bound dimer structure of a b-Hairpin antimicrobial peptide from rotational-echo double-resonance solidstate NMR. Biochemistry 45(27):8341-8349 (Pubitemid 44036540)
    • (2006) Biochemistry , vol.45 , Issue.27 , pp. 8341-8349
    • Mani, R.1    Tang, M.2    Wu, X.3    Buffy, J.J.4    Waring, A.J.5    Sherman, M.A.6    Hong, M.7
  • 29
    • 41149160723 scopus 로고    scopus 로고
    • 13C spin-diffusion solid-state NMR spectroscopy
    • DOI 10.1021/ja078039s
    • Manolikas T, Herrmann T, Meier BH (2008) Protein structure determination from C-13 spin-diffusion solid-state NMR spectroscopy. J Am Chem Soc 130(12):3959-3966 (Pubitemid 351429863)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.12 , pp. 3959-3966
    • Manolikas, T.1    Herrmann, T.2    Meier, B.H.3
  • 31
    • 69949160677 scopus 로고    scopus 로고
    • Atomic resolution protein structure determination by threedimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy
    • Nieuwkoop AJ, Wylie BJ, Franks WT, Shah GJ, Rienstra CM (2009) Atomic resolution protein structure determination by threedimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy. J Chem Phys 131(9):095101
    • (2009) J Chem Phys , vol.131 , Issue.9 , pp. 095101
    • Nieuwkoop, A.J.1    Wylie, B.J.2    Franks, W.T.3    Shah, G.J.4    Rienstra, C.M.5
  • 32
    • 79953051538 scopus 로고    scopus 로고
    • Solid-state NMR on a large multidomain integral membrane protein: The outer membrane protein assembly factor Bam A
    • Renault M, Bos MP, Tommassen J, Baldus M (2011) Solid-state NMR on a large multidomain integral membrane protein: the outer membrane protein assembly factor Bam A. J Am Chem Soc 133(12):4175-4177
    • (2011) J Am Chem Soc , vol.133 , Issue.12 , pp. 4175-4177
    • Renault, M.1    Bos, M.P.2    Tommassen, J.3    Baldus, M.4
  • 33
    • 36549022966 scopus 로고    scopus 로고
    • Operator-based triple-mode Floquet theory in solid-state NMR
    • Scholz I, Meier BH, Ernst M(2007) Operator-based triple-mode Floquet theory in solid-state NMR. J Chem Phys 127(20):204504-204513
    • (2007) J Chem Phys , vol.127 , Issue.20 , pp. 204504-204513
    • Scholz, I.1    Meier, B.H.2    Ernst, M.3
  • 35
  • 36
    • 67649865606 scopus 로고    scopus 로고
    • Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach
    • Traaseth NJ, Shi L, Verardi R, Mullen DG, Barany G, Veglia G (2009) Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach. Proc Natl Acad Sci USA 106(25):10165-10170
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.25 , pp. 10165-10170
    • Traaseth, N.J.1    Shi, L.2    Verardi, R.3    Mullen, D.G.4    Barany, G.5    Veglia, G.6
  • 37
    • 77957324146 scopus 로고    scopus 로고
    • Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy
    • van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, Böckmann A, Meier BH (2010) Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy. J Am Chem Soc 132(39):13765-13775
    • (2010) J Am Chem Soc , vol.132 , Issue.39 , pp. 13765-13775
    • Van Melckebeke, H.1    Wasmer, C.2    Lange, A.3    Ab, E.4    Loquet, A.5    Böckmann, A.6    Meier, B.H.7
  • 38
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core
    • DOI 10.1126/science.1151839
    • Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH (2008) Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 319(5869):1523-1526 (Pubitemid 351398180)
    • (2008) Science , vol.319 , Issue.5869 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 39
    • 77349106883 scopus 로고    scopus 로고
    • Resonance assignment and three-dimensional structure determination of a human a-defensin, HNP-1, by solid-state NMR
    • Zhang Y, Doherty T, Li J, Lu W, Barinka C, Lubkowski J, Hong M (2010) Resonance assignment and three-dimensional structure determination of a human a-defensin, HNP-1, by solid-state NMR. J Mol Biol 397(2):408-422
    • (2010) J Mol Biol , vol.397 , Issue.2 , pp. 408-422
    • Zhang, Y.1    Doherty, T.2    Li, J.3    Lu, W.4    Barinka, C.5    Lubkowski, J.6    Hong, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.