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Volumn 43, Issue 4, 2009, Pages 247-254

Intermolecular dynamics studied by paramagnetic tagging

Author keywords

Dynamics; Encounter complex; Lanthanide tag; Paramagnetic NMR; Residual dipolar couplings

Indexed keywords

ADRENODOXIN; CYTOCHROME C; LANTHANIDE;

EID: 63449111236     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-009-9308-0     Document Type: Article
Times cited : (47)

References (41)
  • 1
    • 0032539192 scopus 로고    scopus 로고
    • 5 at high magnetic fields: Magnetic susceptibility anisotropy contributions and consequences for protein solution structure determination
    • 5 at high magnetic fields: Magnetic susceptibility anisotropy contributions and consequences for protein solution structure determination. J Am Chem Soc 120:12903-12909
    • (1998) J Am Chem Soc , vol.120 , pp. 12903-12909
    • Banci, L.1    Bertini, I.2    Huber, J.G.3    Luchinat, C.4    Rosato, A.5
  • 4
    • 25844506708 scopus 로고    scopus 로고
    • Weak alignment NMR: A hawk-eyed view of biomolecular structure
    • Bax A, Grishaev A (2005) Weak alignment NMR: A hawk-eyed view of biomolecular structure. Curr Opin Struct Biol 15:563-570
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 563-570
    • Bax, A.1    Grishaev, A.2
  • 6
    • 35548988910 scopus 로고    scopus 로고
    • Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains
    • Bertini I, Gupta YK, Luchinat C, Parigi G, Peana M, Sgheri L, Yuan J (2007) Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains. J Am Chem Soc 129:12786-12794
    • (2007) J Am Chem Soc , vol.129 , pp. 12786-12794
    • Bertini, I.1    Gupta, Y.K.2    Luchinat, C.3    Parigi, G.4    Peana, M.5    Sgheri, L.6    Yuan, J.7
  • 7
    • 14844363428 scopus 로고    scopus 로고
    • Protein backbone dynamics from N-H-N dipolar couplings in partially aligned systems: A comparison of motional models in the presence of structural noise
    • Bouvignies G, Bernadó P, Blackledge M (2005) Protein backbone dynamics from N-H-N dipolar couplings in partially aligned systems: A comparison of motional models in the presence of structural noise. J Magn Reson 173:328-338
    • (2005) J Magn Reson , vol.173 , pp. 328-338
    • Bouvignies, G.1    Bernadó, P.2    Blackledge, M.3
  • 8
    • 0037186549 scopus 로고    scopus 로고
    • Structure and dynamics of KH domains from FBP bound to single-stranded DNA
    • Braddock DT, Louis JM, Baber JL, Levens D, Clore GM (2002) Structure and dynamics of KH domains from FBP bound to single-stranded DNA. Nature 415:1051-1056
    • (2002) Nature , vol.415 , pp. 1051-1056
    • Braddock, D.T.1    Louis, J.M.2    Baber, J.L.3    Levens, D.4    Clore, G.M.5
  • 9
    • 0036903969 scopus 로고    scopus 로고
    • The ternary complex of cytochrome f and cytochrome c: Identification of a second binding site and competition for plastocyanin binding
    • Crowley PB, Rabe KS, Worrall JAR, Canters GW, Ubbink M (2002) The ternary complex of cytochrome f and cytochrome c: Identification of a second binding site and competition for plastocyanin binding. Chembiochem 3:526-533
    • (2002) Chembiochem , vol.3 , pp. 526-533
    • Crowley, P.B.1    Rabe, K.S.2    Worrall, J.A.R.3    Canters, G.W.4    Ubbink, M.5
  • 11
    • 0034515845 scopus 로고    scopus 로고
    • Ansig for Windows: An interactive computer program for semiautomatic assignment of protein NMR spectra
    • Helgstrand M, Kraulis P, Allard P, Härd T (2000) Ansig for Windows: an interactive computer program for semiautomatic assignment of protein NMR spectra. J Biomol NMR 18:329-336
    • (2000) J Biomol NMR , vol.18 , pp. 329-336
    • Helgstrand, M.1    Kraulis, P.2    Allard, P.3    Härd, T.4
  • 12
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain-reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR (1989) Site-directed mutagenesis by overlap extension using the polymerase chain-reaction. Gene 77:51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 13
    • 0002672994 scopus 로고
    • Single-crystal neutron diffractometry
    • In: Domenicano A, Hargittai I (eds) Oxford University Press, Oxford
    • Jeffrey G (1992) Single-crystal neutron diffractometry. In: Domenicano A, Hargittai I (eds) Accurate molecular structure, their determination and importance. Oxford University Press, Oxford, pp 270-298
    • (1992) Accurate Molecular Structure, Their Determination and Importance , pp. 270-298
    • Jeffrey, G.1
  • 14
    • 34547657260 scopus 로고    scopus 로고
    • Increased paramagnetic effect of a lanthanide protein probe by two-point attachment
    • Keizers PHJ, Desreux JF, Overhand M, Ubbink M (2007) Increased paramagnetic effect of a lanthanide protein probe by two-point attachment. J Am Chem Soc 129:9292-9293
    • (2007) J Am Chem Soc , vol.129 , pp. 9292-9293
    • Keizers, P.H.J.1    Desreux, J.F.2    Overhand, M.3    Ubbink, M.4
  • 15
    • 55549133637 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of a lanthanide chelating protein probe: CLaNP-5 yields predictable paramagnetic effects independent of environment
    • Keizers PH, Saragliadis A, Hiruma Y, Overhand M, Ubbink M (2008) Design, synthesis, and evaluation of a lanthanide chelating protein probe: CLaNP-5 yields predictable paramagnetic effects independent of environment. J Am Chem Soc 130:14802-14812
    • (2008) J Am Chem Soc , vol.130 , pp. 14802-14812
    • Keizers, P.H.1    Saragliadis, A.2    Hiruma, Y.3    Overhand, M.4    Ubbink, M.5
  • 16
    • 42449102160 scopus 로고    scopus 로고
    • Probing invisible, low-populated states of protein molecules by relaxation dispersion NMR spectroscopy: An application to protein folding
    • Korzhnev DM, Kay LE (2008) Probing invisible, low-populated states of protein molecules by relaxation dispersion NMR spectroscopy: An application to protein folding. Acc Chem Res 41:442-451
    • (2008) Acc Chem Res , vol.41 , pp. 442-451
    • Korzhnev, D.M.1    Kay, L.E.2
  • 20
    • 0025146477 scopus 로고
    • High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c
    • Louie GV, Brayer GD (1990) High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c. J Mol Biol 214:527-555
    • (1990) J Mol Biol , vol.214 , pp. 527-555
    • Louie, G.V.1    Brayer, G.D.2
  • 21
    • 0032520951 scopus 로고    scopus 로고
    • New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108)
    • Müller A, Müller J, Müller Y, Uhlman H, Bernhard R, Heineman (1998) New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108). Structure 6:269-280
    • (1998) Structure , vol.6 , pp. 269-280
    • Müller, A.1    Müller, J.2    Müller, Y.3    Uhlman, H.4    Bernhard, R.5    Heineman, U.6
  • 22
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • Ottiger M, Delaglio F, Bax A (1998) Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J Magn Reson 131:373-378
    • (1998) J Magn Reson , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 23
    • 48749105838 scopus 로고    scopus 로고
    • Prospects for lanthanides in structural biology by NMR
    • Otting G (2008) Prospects for lanthanides in structural biology by NMR. J Biomol NMR 42:1-9
    • (2008) J Biomol NMR , vol.42 , pp. 1-9
    • Otting, G.1
  • 24
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • Palmer AG (2004) NMR characterization of the dynamics of biomacromolecules. Chem Rev 104:3623-3640
    • (2004) Chem Rev , vol.104 , pp. 3623-3640
    • Palmer, A.G.1
  • 27
    • 33751086423 scopus 로고    scopus 로고
    • Visualization of transient encounter complexes in protein-protein association
    • Tang C, Iwahara J, Clore GM (2006) Visualization of transient encounter complexes in protein-protein association. Nature 444:383-386
    • (2006) Nature , vol.444 , pp. 383-386
    • Tang, C.1    Iwahara, J.2    Clore, G.M.3
  • 28
    • 35548976322 scopus 로고    scopus 로고
    • Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
    • Tang C, Schwieters CD, Clore GM (2007) Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR. Nature 449:1078-1082
    • (2007) Nature , vol.449 , pp. 1078-1082
    • Tang, C.1    Schwieters, C.D.2    Clore, G.M.3
  • 29
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra N, Bax A (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278:1111-1114
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 30
    • 0030612335 scopus 로고    scopus 로고
    • Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution
    • Tjandra N, Omichinski JG, Gronenborn AM, Clore GM, Bax A (1997) Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution. Nat Struct Biol 4:732-738
    • (1997) Nat Struct Biol , vol.4 , pp. 732-738
    • Tjandra, N.1    Omichinski, J.G.2    Gronenborn, A.M.3    Clore, G.M.4    Bax, A.5
  • 31
    • 33646931175 scopus 로고    scopus 로고
    • NMR residual dipolar couplings as probes of biomolecular dynamics
    • Tolman JR, Ruan K (2006) NMR residual dipolar couplings as probes of biomolecular dynamics. Chem Rev 106:1720-1736
    • (2006) Chem Rev , vol.106 , pp. 1720-1736
    • Tolman, J.R.1    Ruan, K.2
  • 32
    • 0029050883 scopus 로고
    • Nuclear magnetic dipole interactions in field-oriented proteins - Information for structure determination in solution
    • Tolman JR, Flanagan JM, Kennedy MA, Prestegard JH (1995) Nuclear magnetic dipole interactions in field-oriented proteins - information for structure determination in solution. Proc Natl Acad Sci USA 92:9279-9283
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9279-9283
    • Tolman, J.R.1    Flanagan, J.M.2    Kennedy, M.A.3    Prestegard, J.H.4
  • 33
    • 0030990022 scopus 로고    scopus 로고
    • Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis
    • Ubbink M, Bendall DS (1997) Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis. Biochemistry 36:6326-6335
    • (1997) Biochemistry , vol.36 , pp. 6326-6335
    • Ubbink, M.1    Bendall, D.S.2
  • 34
    • 0036652846 scopus 로고    scopus 로고
    • SH3-SH2 domain orientation in Src kinases: NMR studies of Fyn
    • Ulmer TS, Werner JM, Campbell ID (2002) SH3-SH2 domain orientation in Src kinases: NMR studies of Fyn. Structure 10:901-911
    • (2002) Structure , vol.10 , pp. 901-911
    • Ulmer, T.S.1    Werner, J.M.2    Campbell, I.D.3
  • 35
    • 14144250394 scopus 로고    scopus 로고
    • The orientations of cytochrome c in the highly dynamic complex with cytochrome b 5 visualized by NMR and docking using HADDOCK
    • Volkov AN, Ferrari D, Worrall JAR, Bonvin AMJJ, Ubbink M (2005) The orientations of cytochrome c in the highly dynamic complex with cytochrome b 5 visualized by NMR and docking using HADDOCK. Protein Sci 14:799-811
    • (2005) Protein Sci , vol.14 , pp. 799-811
    • Volkov, A.N.1    Ferrari, D.2    Worrall, J.A.R.3    Bonvin, A.M.J.J.4    Ubbink, M.5
  • 36
    • 34250838027 scopus 로고    scopus 로고
    • Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR
    • Volkov AN, Worrall JAR, Holtzmann E, Ubbink M (2006) Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR. Proc Natl Acad Sci USA 103:18945-18950
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18945-18950
    • Volkov, A.N.1    Worrall, J.A.R.2    Holtzmann, E.3    Ubbink, M.4
  • 39
    • 0038470801 scopus 로고    scopus 로고
    • Transient protein interactions studied by NMR spectroscopy: The case of cytochrome c and adrenodoxin
    • Worrall JAR, Reinle W, Bernhardt R, Ubbink M (2003) Transient protein interactions studied by NMR spectroscopy: The case of cytochrome c and adrenodoxin. Biochemistry 42:7068-7076
    • (2003) Biochemistry , vol.42 , pp. 7068-7076
    • Worrall, J.A.R.1    Reinle, W.2    Bernhardt, R.3    Ubbink, M.4
  • 40
    • 43949086199 scopus 로고    scopus 로고
    • Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy
    • Xu XF, Reinle WG, Hannemann F, Konarev PV, Svergun DI, Bernhardt R, Ubbink M (2008) Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy. J Am Chem Soc 130:6395-6403
    • (2008) J Am Chem Soc , vol.130 , pp. 6395-6403
    • Xu, X.F.1    Reinle, W.G.2    Hannemann, F.3    Konarev, P.V.4    Svergun, D.I.5    Bernhardt, R.6    Ubbink, M.7
  • 41
    • 37549017736 scopus 로고    scopus 로고
    • Visualizing spatially correlated dynamics that directs RNA conformational transitions
    • Zhang Q, Stelzer AC, Fisher CK, Al-Hashimi HM (2007) Visualizing spatially correlated dynamics that directs RNA conformational transitions. Nature 450:1263-1267
    • (2007) Nature , vol.450 , pp. 1263-1267
    • Zhang, Q.1    Stelzer, A.C.2    Fisher, C.K.3    Al-Hashimi, H.M.4


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