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Volumn 178, Issue 1, 2006, Pages 72-76

Effective rotational correlation times of proteins from NMR relaxation interference

Author keywords

Brownian motion; Cross correlated relaxation; Effective rotational correlation time; NMR; TROSY

Indexed keywords

AGGLOMERATION; ANISOTROPY; BROWNIAN MOVEMENT; CORRELATION METHODS; ESCHERICHIA COLI; MACROMOLECULES; ROTATION; SAMPLING;

EID: 28844480494     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2005.08.014     Document Type: Article
Times cited : (216)

References (27)
  • 2
    • 0000961515 scopus 로고    scopus 로고
    • Technical aspects of NMR spectroscopy with biological macromolecules and studies of hydration in solution
    • G. Wider Technical aspects of NMR spectroscopy with biological macromolecules and studies of hydration in solution Prog. Nucl. Magn. Reson. Spectrosc. 32 1998 193 275
    • (1998) Prog. Nucl. Magn. Reson. Spectrosc. , vol.32 , pp. 193-275
    • Wider, G.1
  • 4
    • 0034328380 scopus 로고    scopus 로고
    • HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations
    • J.G. de la Torre, M.L. Huertas, and B. Carrasco HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations J. Magn. Reson. 147 2000 138 146
    • (2000) J. Magn. Reson. , vol.147 , pp. 138-146
    • De La Torre, J.G.1    Huertas, M.L.2    Carrasco, B.3
  • 5
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to Staphylococcal nuclease
    • 15N inverse detected heteronuclear NMR spectroscopy: application to Staphylococcal nuclease Biochemistry 28 1989 8972 8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 7
    • 0032511359 scopus 로고    scopus 로고
    • 15N chemical shift anisotropy relaxation interference: Unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules
    • 15N chemical shift anisotropy relaxation interference: unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules J. Am. Chem. Soc. 120 1998 7905 7915
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7905-7915
    • Kroenke, C.D.1    Loria, J.P.2    Lee, L.K.3    Rance, M.4    Palmer, A.G.5
  • 8
    • 0037192915 scopus 로고    scopus 로고
    • Semi-classical nuclear spin relaxation theory revisited for use with biological macromolecules
    • P. Luginbühl, and K. Wüthrich Semi-classical nuclear spin relaxation theory revisited for use with biological macromolecules Prog. Nucl. Magn. Reson. Spectrosc. 40 2002 199 247
    • (2002) Prog. Nucl. Magn. Reson. Spectrosc. , vol.40 , pp. 199-247
    • Luginbühl, P.1    Wüthrich, K.2
  • 9
    • 0030612833 scopus 로고    scopus 로고
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution Proc. Natl. Acad. Sci. USA 94 1997 12366 12371
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 10
    • 0007133861 scopus 로고
    • Cross-correlation between dipolar and chemical-shift anisotropy interaction-application to anisotropic rotational diffusion
    • G. Kontaxis, N. Müller, and H. Sterk Cross-correlation between dipolar and chemical-shift anisotropy interaction-application to anisotropic rotational diffusion J. Magn. Reson. 92 1991 332 341
    • (1991) J. Magn. Reson. , vol.92 , pp. 332-341
    • Kontaxis, G.1    Müller, N.2    Sterk, H.3
  • 11
    • 0034241349 scopus 로고    scopus 로고
    • 1H dipole-dipole relaxation cross-correlation experiments
    • 1H dipole-dipole relaxation cross-correlation experiments J. Magn. Reson. 145 2000 192 200
    • (2000) J. Magn. Reson. , vol.145 , pp. 192-200
    • Renner, C.1    Holak, T.A.2
  • 12
    • 48549112585 scopus 로고
    • Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei
    • M. Goldman Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei J. Magn. Reson. 60 1984 437 452
    • (1984) J. Magn. Reson. , vol.60 , pp. 437-452
    • Goldman, M.1
  • 15
    • 0034146355 scopus 로고    scopus 로고
    • Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times
    • G. Kontaxis, G.M. Clore, and A. Bax Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times J. Magn. Reson. 143 2000 184 196
    • (2000) J. Magn. Reson. , vol.143 , pp. 184-196
    • Kontaxis, G.1    Clore, G.M.2    Bax, A.3
  • 16
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • G. Lipari, and A. Szabo Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity J. Am. Chem. Soc. 104 1982 4546 4559
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 17
    • 0142149113 scopus 로고    scopus 로고
    • Stereospecific assignments of the isopropyl methyl groups of the membrane protein OmpX in DHPC micelles
    • C. Hilty, G. Wider, C. Fernández, and K. Wüthrich Stereospecific assignments of the isopropyl methyl groups of the membrane protein OmpX in DHPC micelles J. Biomol. NMR 27 2003 377 382
    • (2003) J. Biomol. NMR , vol.27 , pp. 377-382
    • Hilty, C.1    Wider, G.2    Fernández, C.3    Wüthrich, K.4
  • 18
    • 0035979788 scopus 로고    scopus 로고
    • Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli
    • C. Fernández, C. Hilty, S. Bonjour, K. Adeishvili, K. Pervushin, and K. Wüthrich Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli FEBS Lett. 504 2001 173 178
    • (2001) FEBS Lett. , vol.504 , pp. 173-178
    • Fernández, C.1    Hilty, C.2    Bonjour, S.3    Adeishvili, K.4    Pervushin, K.5    Wüthrich, K.6
  • 19
    • 0036700404 scopus 로고    scopus 로고
    • Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles
    • C. Hilty, C. Fernández, G. Wider, and K. Wüthrich Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles J. Biomol. NMR 23 2002 289 301
    • (2002) J. Biomol. NMR , vol.23 , pp. 289-301
    • Hilty, C.1    Fernández, C.2    Wider, G.3    Wüthrich, K.4
  • 20
    • 0035956956 scopus 로고    scopus 로고
    • Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles
    • C. Fernández, K. Adeishvili, and K. Wüthrich Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles Proc. Natl. Acad. Sci. USA 98 2001 2358 2363
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2358-2363
    • Fernández, C.1    Adeishvili, K.2    Wüthrich, K.3
  • 21
    • 0034625918 scopus 로고    scopus 로고
    • NMR assignment and secondary structure determination of an octameric 110 kDa protein using TROSY in triple resonance experiments
    • M. Salzmann, K. Pervushin, G. Wider, H. Senn, and K. Wüthrich NMR assignment and secondary structure determination of an octameric 110 kDa protein using TROSY in triple resonance experiments J. Am. Chem. Soc. 122 2000 7543 7548
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 7543-7548
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wüthrich, K.5
  • 22
    • 0037032418 scopus 로고    scopus 로고
    • NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH
    • D. Lee, F.F. Damberger, and G.H. Peng NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH FEBS Lett. 531 2002 314 318
    • (2002) FEBS Lett. , vol.531 , pp. 314-318
    • Lee, D.1    Damberger, F.F.2    Peng, G.H.3
  • 23
    • 0037120882 scopus 로고    scopus 로고
    • Solution NMR techniques for large molecular and supramolecular structures
    • R. Riek, J. Fiaux, E.B. Bertelsen, A.L. Horwich, and K. Wüthrich Solution NMR techniques for large molecular and supramolecular structures J. Am. Chem. Soc. 124 2002 12144 12153
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12144-12153
    • Riek, R.1    Fiaux, J.2    Bertelsen, E.B.3    Horwich, A.L.4    Wüthrich, K.5
  • 24
    • 0000486802 scopus 로고
    • Suppression of the effects of cross-correlation between dipolar and anisotropic chemical-shift relaxation mechanisms in the measurement of spin-spin relaxation rates
    • A.G. Palmer, N.J. Skelton, W.J. Chazin, P.E. Wright, and M. Rance Suppression of the effects of cross-correlation between dipolar and anisotropic chemical-shift relaxation mechanisms in the measurement of spin-spin relaxation rates Mol. Phys. 75 1992 699 711
    • (1992) Mol. Phys. , vol.75 , pp. 699-711
    • Palmer, A.G.1    Skelton, N.J.2    Chazin, W.J.3    Wright, P.E.4    Rance, M.5
  • 25
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • L.E. Kay, P. Keifer, and T. Saarinen Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity J. Am. Chem. Soc. 114 1992 10663 10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 27
    • 0001444750 scopus 로고
    • Measurement of heteronuclear bond distances in polycrystalline solids by solid-State NMR Techniques
    • J.E. Roberts, G.S. Harbison, M.G. Munowitz, J. Herzfeld, and R.G. Griffin Measurement of heteronuclear bond distances in polycrystalline solids by solid-State NMR Techniques J. Am. Chem. Soc. 109 1987 4163 4169
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 4163-4169
    • Roberts, J.E.1    Harbison, G.S.2    Munowitz, M.G.3    Herzfeld, J.4    Griffin, R.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.