메뉴 건너뛰기




Volumn 57, Issue 2, 2013, Pages 129-139

Selectively dispersed isotope labeling for protein structure determination by magic angle spinning NMR

Author keywords

13C acetate; Dipolar truncation; Isotope labeled peptone; Isotope substitution; MAS NMR structure determination; Sparse labeling

Indexed keywords

ACETIC ACID; AMINO ACID; BINDING PROTEIN; CARBON 13; CARBOXYL GROUP; IMMUNOGLOBULIN BINDING PROTEIN G; PEPTONE; UNCLASSIFIED DRUG;

EID: 84892935089     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-013-9773-3     Document Type: Article
Times cited : (23)

References (45)
  • 1
    • 0025234587 scopus 로고
    • PH-Induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson D, Becktel W, Dahlquist F (1990) pH-Induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 29(9): 2403-2408
    • (1990) Biochemistry , vol.29 , Issue.9 , pp. 2403-2408
    • Anderson, D.1    Becktel, W.2    Dahlquist, F.3
  • 2
    • 41449085042 scopus 로고    scopus 로고
    • Radio frequency-driven recoupling at high magic-angle spinning frequencies: Homonuclear recoupling sans heteronuclear decoupling
    • doi:10.1063/1.2834736
    • Bayro MJ, Ramachandran R, Caporini MA, Eddy MT, Griffin RG (2008) Radio frequency-driven recoupling at high magic-angle spinning frequencies: homonuclear recoupling sans heteronuclear decoupling. J Chem Phys 128(5):052321. doi:10.1063/1.2834736
    • (2008) J Chem Phys , vol.128 , Issue.5 , pp. 052321
    • Bayro, M.J.1    Ramachandran, R.2    Caporini, M.A.3    Eddy, M.T.4    Griffin, R.G.5
  • 4
    • 77956158248 scopus 로고    scopus 로고
    • High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: Backbone conformation and implications for protofilament assembly and structure
    • doi:10.1021/bi100864t
    • Bayro MJ, Maly T, Birkett NR, Macphee CE, Dobson CM, Griffin RG (2010) High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation and Implications for Protofilament Assembly and Structure. Biochemistry 49(35): 7474-7484. doi:10.1021/bi100864t
    • (2010) Biochemistry , vol.49 , Issue.35 , pp. 7474-7484
    • Bayro, M.J.1    Maly, T.2    Birkett, N.R.3    Macphee, C.E.4    Dobson, C.M.5    Griffin, R.G.6
  • 5
    • 80052335544 scopus 로고    scopus 로고
    • Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR
    • Bayro M, Debelouchina G, Eddy M, Birkett N, MacPhee C, Rosay M, Maas W, Dobson C, Griffin R (2011) Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR. J Am Chem Soc 133(35): 13967-13974
    • (2011) J Am Chem Soc , vol.133 , Issue.35 , pp. 13967-13974
    • Bayro, M.1    Debelouchina, G.2    Eddy, M.3    Birkett, N.4    Macphee, C.5    Rosay, M.6    Maas, W.7    Dobson, C.8    Griffin, R.9
  • 8
    • 0037038365 scopus 로고    scopus 로고
    • Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
    • Castellani F, van Rossum B, Diehl A, Schubert M, Rehbein K, Oschkinat H (2002) Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy. Nature 420(6911): 98-102
    • (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    Oschkinat, H.6
  • 9
    • 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
    • doi:10.1021/bi034903r
    • Castellani F, van Rossum B-J, Diehl A, Rehbein K, Oschkinat H (2003) Determination of solid-state NMR structures of proteins by means of three-dimensional 15N-13C-13C dipolar correlation spectroscopy and chemical shift analysis. Biochemistry 42(39):11476-11483. doi:10.1021/bi034903r
    • (2003) Biochemistry , vol.42 , Issue.39 , pp. 11476-11483
    • Castellani, F.1    Van Rossum, B.-J.2    Diehl, A.3    Rehbein, K.4    Oschkinat, H.5
  • 12
    • 0030981715 scopus 로고    scopus 로고
    • Carbonyl carbon probe of local mobility in 13C, 15N-enriched proteins using high-resolution nuclear magnetic resonance
    • Dayie K, Wagner G (1997) Carbonyl carbon probe of local mobility in 13C, 15N-enriched proteins using high-resolution nuclear magnetic resonance. J Am Chem Soc 119(33):7797-7806
    • (1997) J Am Chem Soc , vol.119 , Issue.33 , pp. 7797-7806
    • Dayie, K.1    Wagner, G.2
  • 14
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister G, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277-293
    • (1995) J Biomol NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 15
    • 33846430490 scopus 로고    scopus 로고
    • Secondary structure, dynamics, and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy
    • doi:10.1002/anie.200602139
    • Etzkorn M, Martell S, Andronesi OC, Seidel K, Engelhard M, Baldus M (2007) Secondary structure, dynamics, and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy. Angew Chem Int Ed 46(3):459-462. doi:10.1002/anie.200602139
    • (2007) Angew Chem Int Ed , vol.46 , Issue.3 , pp. 459-462
    • Etzkorn, M.1    Martell, S.2    Andronesi, O.C.3    Seidel, K.4    Engelhard, M.5    Baldus, M.6
  • 16
    • 24644462659 scopus 로고    scopus 로고
    • Magic-angle spinning solidstate NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis
    • doi:10.1021/ja044497e
    • Franks WT, Zhou DH, Wylie BJ, Money BG, Graesser DT, Frericks HL, Sahota G, Rienstra CM (2005) Magic-angle spinning solidstate NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis. J Am Chem Soc 127(35):12291-12305. doi:10.1021/ja044497e
    • (2005) J Am Chem Soc , vol.127 , Issue.35 , pp. 12291-12305
    • Franks, W.T.1    Zhou, D.H.2    Wylie, B.J.3    Money, B.G.4    Graesser, D.T.5    Frericks, H.L.6    Sahota, G.7    Rienstra, C.M.8
  • 17
    • 33644942810 scopus 로고    scopus 로고
    • Backbone conformational constraints in a microcrystalline U-15N-labeled protein by 3D dipolar-shift solid-state NMR spectroscopy
    • doi:10.1021/ja058292x
    • Franks WT, Wylie BJ, Stellfox SA, Rienstra CM (2006) Backbone conformational constraints in a microcrystalline U-15N-labeled protein by 3D dipolar-shift solid-state NMR spectroscopy. J Am Chem Soc 128(10):3154-3155. doi:10.1021/ja058292x
    • (2006) J Am Chem Soc , vol.128 , Issue.10 , pp. 3154-3155
    • Franks, W.T.1    Wylie, B.J.2    Stellfox, S.A.3    Rienstra, C.M.4
  • 18
    • 35748970172 scopus 로고    scopus 로고
    • Assignment of congested NMR spectra: Carbonyl backbone enrichment via the Entner-Doudoroff pathway
    • doi:10.1016/j.jmr.2007.07.011
    • Goldbourt A, Day LA, McDermott AE (2007) Assignment of congested NMR spectra: carbonyl backbone enrichment via the Entner-Doudoroff pathway. J Magn Reson 189(2):157-165. doi:10.1016/j.jmr.2007.07.011
    • (2007) J Magn Reson , vol.189 , Issue.2 , pp. 157-165
    • Goldbourt, A.1    Day, L.A.2    McDermott, A.E.3
  • 19
    • 77749237271 scopus 로고    scopus 로고
    • Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy
    • doi:10.1021/ja909827v
    • Helmus JJ, Surewicz K, Surewicz WK, Jaroniec CP (2010) Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy. J Am Chem Soc 132(7):2393-2403. doi:10.1021/ja909827v
    • (2010) J Am Chem Soc , vol.132 , Issue.7 , pp. 2393-2403
    • Helmus, J.J.1    Surewicz, K.2    Surewicz, W.K.3    Jaroniec, C.P.4
  • 20
    • 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
    • doi:10.1007/s10858-009-9338-7
    • Higman VA, Flinders J, Hiller M, Jehle S, Markovic S, Fiedler S, 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. doi:10.1007/s10858-009-9338-7
    • (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    Rossum, B.-J.7    Oschkinat, H.8
  • 21
    • 40149084899 scopus 로고    scopus 로고
    • 2,3-(13)C]-labeling of aromatic residues-getting a head start in the magic-angle-spinning NMR assignment of membrane proteins
    • doi:10.1021/ja077589n
    • Hiller M, Higman VA, Jehle S, van Rossum B-J, Kühlbrandt W, Oschkinat H (2008) [2,3-(13)C]-labeling of aromatic residues-getting a head start in the magic-angle-spinning NMR assignment of membrane proteins. J Am Chem Soc 130(2):408-409. doi:10.1021/ja077589n
    • (2008) J Am Chem Soc , vol.130 , Issue.2 , pp. 408-409
    • Hiller, M.1    Higman, V.A.2    Jehle, S.3    Van Rossum, B.-J.4    Kühlbrandt, W.5    Oschkinat, H.6
  • 22
    • 0000414471 scopus 로고
    • Transferred-echo doubleresonance NMR
    • Hing WA, Vega S, Schaefer J (1992) Transferred-echo doubleresonance NMR. J Magn Reson 96(1):205-209
    • (1992) J Magn Reson , vol.96 , Issue.1 , pp. 205-209
    • Hing, W.A.1    Vega, S.2    Schaefer, J.3
  • 23
    • 0033170449 scopus 로고    scopus 로고
    • Determination of multiple phi-torsion angles in proteins by selective and extensive 13C labeling and twodimensional solid-state NMR
    • Hong M (1999) Determination of multiple phi-torsion angles in proteins by selective and extensive 13C labeling and twodimensional solid-state NMR. J Magn Reson 139(2):389-401
    • (1999) J Magn Reson , vol.139 , Issue.2 , pp. 389-401
    • Hong, M.1
  • 24
    • 0033543134 scopus 로고    scopus 로고
    • Backbone dynamics of the N-terminal domain in E. Coli DnaJ determined by 15N- and 13CO-relaxation measurements
    • Huang K, Ghose R, Flanagan J, Prestegard J (1999) Backbone dynamics of the N-terminal domain in E. coli DnaJ determined by 15N- and 13CO-relaxation measurements. Biochemistry 38(32):10567-10577
    • (1999) Biochemistry , vol.38 , Issue.32 , pp. 10567-10577
    • Huang, K.1    Ghose, R.2    Flanagan, J.3    Prestegard, J.4
  • 25
    • 77957005819 scopus 로고
    • Crystallization as a purification technique
    • Jakoby WB (1971) Crystallization as a purification technique. Methods Enzymol 22:248-252
    • (1971) Methods Enzymol , vol.22 , pp. 248-252
    • Jakoby, W.B.1
  • 26
    • 75749091094 scopus 로고    scopus 로고
    • Interresidue carbonyl-carbonyl polarization transfer experiments in uniformly 13C, 15N-labeled peptides and proteins
    • doi:10.1016/j.jmr.2009.12.014
    • Janik R, Ritz E, Gravelle A, Shi L, Peng X, Ladizhansky V (2010) Interresidue carbonyl-carbonyl polarization transfer experiments in uniformly 13C, 15N-labeled peptides and proteins. J Magn Reson 203(1):177-184. doi:10.1016/j.jmr.2009.12.014
    • (2010) J Magn Reson , vol.203 , Issue.1 , pp. 177-184
    • Janik, R.1    Ritz, E.2    Gravelle, A.3    Shi, L.4    Peng, X.5    Ladizhansky, V.6
  • 27
    • 0037063498 scopus 로고    scopus 로고
    • 3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly (13)C, (15)N-labeled solids
    • Jaroniec CP, Filip C, Griffin RG (2002) 3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly (13)C, (15)N-labeled solids. J Am Chem Soc 124(36):10728-10742
    • (2002) J Am Chem Soc , vol.124 , Issue.36 , pp. 10728-10742
    • Jaroniec, C.P.1    Filip, C.2    Griffin, R.G.3
  • 28
    • 0033620360 scopus 로고    scopus 로고
    • Comparison of 2H and 13C NMR relaxation techniques for the study of protein methyl group dynamics in solution
    • Lee A, Flynn P, Wand A (1999) Comparison of 2H and 13C NMR relaxation techniques for the study of protein methyl group dynamics in solution. J Am Chem Soc 121(12):2891-2902
    • (1999) J Am Chem Soc , vol.121 , Issue.12 , pp. 2891-2902
    • Lee, A.1    Flynn, P.2    Wand, A.3
  • 29
    • 0029905210 scopus 로고    scopus 로고
    • Dynamical mapping of E. Coli thioredoxin via 13C NMR relaxation analysis
    • LeMaster DM, Kushlan DM (1996) Dynamical mapping of E. coli thioredoxin via 13C NMR relaxation analysis. J Am Chem Soc 118(39):9255-9264
    • (1996) J Am Chem Soc , vol.118 , Issue.39 , pp. 9255-9264
    • Lemaster, D.M.1    Kushlan, D.M.2
  • 30
    • 78049396749 scopus 로고    scopus 로고
    • Supramolecular interactions probed by 13C-13C solid-state NMR spectroscopy
    • Loquet A, Giller K, Becker S, Lange A (2010) Supramolecular interactions probed by 13C-13C solid-state NMR spectroscopy. J Am Chem Soc 132(43):15164-15166
    • (2010) J Am Chem Soc , vol.132 , Issue.43 , pp. 15164-15166
    • Loquet, A.1    Giller, K.2    Becker, S.3    Lange, A.4
  • 31
    • 79953863930 scopus 로고    scopus 로고
    • 13C spin dilution for simplified and complete solid-state NMR resonance assignment of insoluble biological assemblies
    • doi:10.1021/ja200066s
    • Loquet A, Lv G, Giller K, Becker S, Lange A (2011) 13C spin dilution for simplified and complete solid-state NMR resonance assignment of insoluble biological assemblies. J Am Chem Soc 133(13):4722-4725. doi:10.1021/ja200066s
    • (2011) J Am Chem Soc , vol.133 , Issue.13 , pp. 4722-4725
    • Loquet, A.1    Lv, G.2    Giller, K.3    Becker, S.4    Lange, A.5
  • 33
    • 34250903564 scopus 로고    scopus 로고
    • Fractional 13C enrichment of isolated carbons using [1-13C]-or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone COE ± and side-chain methyl positions in proteins
    • Lundstrom P, Teilum K, Carstensen T, Bezsonova I, Wiesner S, Hansen DF, Religa TL, Akke M, Kay LE (2007) Fractional 13C enrichment of isolated carbons using [1-13C]-or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone COE ± and side-chain methyl positions in proteins. J Biomol NMR 38(3):199-212
    • (2007) J Biomol NMR , vol.38 , Issue.3 , pp. 199-212
    • Lundstrom, P.1    Teilum, K.2    Carstensen, T.3    Bezsonova, I.4    Wiesner, S.5    Hansen, D.F.6    Religa, T.L.7    Akke, M.8    Kay, L.E.9
  • 34
    • 84861822461 scopus 로고    scopus 로고
    • Structural comparison of mouse and human a-synuclein amyloid fibrils by solid-state NMR
    • doi:10.1016/j.jmb.2012.04.009
    • Lv G, Kumar A, Giller K, Orcellet ML, Riedel D, Fernández CO, Becker S, Lange A (2012) Structural comparison of mouse and human a-synuclein amyloid fibrils by solid-state NMR. J Mol Biol 420(1-2):99-111. doi:10.1016/j.jmb.2012.04.009
    • (2012) J Mol Biol , vol.420 , Issue.1-2 , pp. 99-111
    • Lv, G.1    Kumar, A.2    Giller, K.3    Orcellet, M.L.4    Riedel, D.5    Fernández, C.O.6    Becker, S.7    Lange, A.8
  • 35
    • 0242299095 scopus 로고    scopus 로고
    • Carbonyl 13C transverse relaxation measurements to sample protein backbone dynamics
    • doi:10.1002/mrc.1252
    • Mulder FAA, Akke M (2003) Carbonyl 13C transverse relaxation measurements to sample protein backbone dynamics. Magn Reson Chem 41(10):853-865. doi:10.1002/mrc.1252
    • (2003) Magn Reson Chem , vol.41 , Issue.10 , pp. 853-865
    • Faa, M.1    Akke, M.2
  • 36
    • 77953118406 scopus 로고    scopus 로고
    • Supramolecular protein structure determination by site-specific long-range intermolecular solid state NMR spectroscopy
    • Nieuwkoop A, Rienstra C (2010) Supramolecular protein structure determination by site-specific long-range intermolecular solid state NMR spectroscopy. J Am Chem Soc 132(22):7570-7571
    • (2010) J Am Chem Soc , vol.132 , Issue.22 , pp. 7570-7571
    • Nieuwkoop, A.1    Rienstra, C.2
  • 37
    • 69949160677 scopus 로고    scopus 로고
    • Atomic resolution protein structure determination by threedimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy
    • doi:10.1063/1.3211103
    • 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. doi:10.1063/1.3211103
    • (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
  • 38
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's b-amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova A, Ishii Y, Balbach J, Antzutkin O, Leapman R, Delaglio F, Tycko R (2002) A structural model for Alzheimer's b-amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci 99(26):16742-16747
    • (2002) Proc Natl Acad Sci , vol.99 , Issue.26 , pp. 16742-16747
    • Petkova, A.1    Ishii, Y.2    Balbach, J.3    Antzutkin, O.4    Leapman, R.5    Delaglio, F.6    Tycko, R.7
  • 39
    • 0034722068 scopus 로고    scopus 로고
    • Parameter optimization for the analysis of underivatized protein amino acids by liquid chromatography and ionspray tandem mass spectrometry
    • Petritis K, Chaimbault P, Elfakir C, Dreux M (2000) Parameter optimization for the analysis of underivatized protein amino acids by liquid chromatography and ionspray tandem mass spectrometry. J Chromatogr A 896(1):253-263
    • (2000) J Chromatogr A , vol.896 , Issue.1 , pp. 253-263
    • Petritis, K.1    Chaimbault, P.2    Elfakir, C.3    Dreux, M.4
  • 40
    • 0036144914 scopus 로고    scopus 로고
    • Rapid determination of underivatized pyroglutamic acid, glutamic acid, glutamine and other relevant amino acids in fermentation media by LC-MS-MS
    • Qu J, Chen W, Luo G, Wang Y, Xiao S, Ling Z, Chen G (2002a) Rapid determination of underivatized pyroglutamic acid, glutamic acid, glutamine and other relevant amino acids in fermentation media by LC-MS-MS. Analyst 127(1):66-69
    • (2002) Analyst , vol.127 , Issue.1 , pp. 66-69
    • Qu, J.1    Chen, W.2    Luo, G.3    Wang, Y.4    Xiao, S.5    Ling, Z.6    Chen, G.7
  • 41
    • 0036558171 scopus 로고    scopus 로고
    • Validated quantification of underivatized amino acids in human blood samples by volatile ion-pair reversed-phase liquid chromatography coupled to isotope dilution tandem mass spectrometry
    • Qu J, Wang Y, Luo G, Wu Z, Yang C (2002b) Validated quantification of underivatized amino acids in human blood samples by volatile ion-pair reversed-phase liquid chromatography coupled to isotope dilution tandem mass spectrometry. Anal Chem 74(9):2034-2040
    • (2002) Anal Chem , vol.74 , Issue.9 , pp. 2034-2040
    • Qu, J.1    Wang, Y.2    Luo, G.3    Wu, Z.4    Yang, C.5
  • 42
    • 38349139799 scopus 로고    scopus 로고
    • Crystal polymorphism of protein GB1 examined by solid-state NMR spectroscopy and X-ray diffraction
    • doi:10.1021/jp075531p
    • Schmidt HLF, Sperling LJ, Gao YG, Wylie BJ, Boettcher JM, Wilson SR, Rienstra CM (2007) Crystal polymorphism of protein GB1 examined by solid-state NMR spectroscopy and X-ray diffraction. J Phys Chem B 111(51):14362-14369. doi:10.1021/jp075531p
    • (2007) J Phys Chem B , vol.111 , Issue.51 , pp. 14362-14369
    • Hlf, S.1    Sperling, L.J.2    Gao, Y.G.3    Wylie, B.J.4    Boettcher, J.M.5    Wilson, S.R.6    Rienstra, C.M.7
  • 43
    • 60149086516 scopus 로고    scopus 로고
    • Three-dimensional solid-state NMR study of a sevenhelical integral membrane proton pump-structural insights
    • Shi L, Ahmed MAM, Zhang W, Whited G, Brown LS, Ladizhansky V (2009) Three-dimensional solid-state NMR study of a sevenhelical integral membrane proton pump-structural insights. J Mol Biol 386(4):1078-1093
    • (2009) J Mol Biol , vol.386 , Issue.4 , pp. 1078-1093
    • Shi, L.1    Mam, A.2    Zhang, W.3    Whited, G.4    Brown, L.S.5    Ladizhansky, V.6
  • 44
    • 77953082958 scopus 로고    scopus 로고
    • Assignment strategies for large proteins by magic-angle spinning NMR: The 21-kDa disulfide-bond-forming enzyme DsbA
    • doi:10.1016/j.jmb.2010.04.012
    • Sperling LJ, Berthold DA, Sasser TL, Jeisy-Scott V, Rienstra CM (2010) Assignment strategies for large proteins by magic-angle spinning NMR: the 21-kDa disulfide-bond-forming enzyme DsbA. J Mol Biol 399(2):268-282. doi:10.1016/j.jmb.2010.04.012
    • (2010) J Mol Biol , vol.399 , Issue.2 , pp. 268-282
    • Sperling, L.J.1    Berthold, D.A.2    Sasser, T.L.3    Jeisy-Scott, V.4    Rienstra, C.M.5
  • 45
    • 0013904956 scopus 로고
    • The aerobic pseudomonas: A taxonomic study
    • Stanier R, Palleroni N, Doudoroff M (1966) The aerobic pseudomonas: a taxonomic study. J Gen Microbiol 43(2):159-271
    • (1966) J Gen Microbiol , vol.43 , Issue.2 , pp. 159-271
    • Stanier, R.1    Palleroni, N.2    Doudoroff, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.