메뉴 건너뛰기




Volumn 136, Issue 2-3, 2008, Pages 145-151

Protein effective rotational correlation times from translational self-diffusion coefficients measured by PFG-NMR

Author keywords

Collective 15N relaxation parameters; Effective rotational correlation time; Hydrodynamic calculations; PFG NMR; Translational diffusion coefficient

Indexed keywords

PROTEIN;

EID: 46049109892     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.06.002     Document Type: Article
Times cited : (33)

References (26)
  • 2
    • 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
  • 5
    • 33751051488 scopus 로고    scopus 로고
    • Structure, dynamics and heparin binding of the C-terminal domain of insulin-like growth factor-binding protein-2 (IGFBP-2)
    • Kuang Z., Yao S., Keizer D.W., Wang C.C., Bach L.A., Forbes B.E., Wallace J.C., and Norton R.S. Structure, dynamics and heparin binding of the C-terminal domain of insulin-like growth factor-binding protein-2 (IGFBP-2). J. Mol. Biol. 364 (2006) 690-704
    • (2006) J. Mol. Biol. , vol.364 , pp. 690-704
    • Kuang, Z.1    Yao, S.2    Keizer, D.W.3    Wang, C.C.4    Bach, L.A.5    Forbes, B.E.6    Wallace, J.C.7    Norton, R.S.8
  • 6
    • 28844480494 scopus 로고    scopus 로고
    • Effective rotational correlation times of proteins from NMR relaxation interference
    • Lee D., Hilty C., Wider G., and Wüthrich K. Effective rotational correlation times of proteins from NMR relaxation interference. J. Magn. Reson. 178 (2006) 72-76
    • (2006) J. Magn. Reson. , vol.178 , pp. 72-76
    • Lee, D.1    Hilty, C.2    Wider, G.3    Wüthrich, K.4
  • 7
    • 0033572679 scopus 로고    scopus 로고
    • Lysozyme aggregation and solution properties studied using PGSE NMR diffusion measurements
    • Price W.S., Tsuchiya F., and Arata Y. Lysozyme aggregation and solution properties studied using PGSE NMR diffusion measurements. J. Am. Chem. Soc. 121 (1999) 11503-11512
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11503-11512
    • Price, W.S.1    Tsuchiya, F.2    Arata, Y.3
  • 8
    • 0034010302 scopus 로고    scopus 로고
    • Peptide self-association in aqueous trifluoroethanol monitored by pulsed field gradient NMR diffusion measurements
    • Yao S., Howlett G.J., and Norton R.S. Peptide self-association in aqueous trifluoroethanol monitored by pulsed field gradient NMR diffusion measurements. J. Biomol. NMR 16 (2000) 109-119
    • (2000) J. Biomol. NMR , vol.16 , pp. 109-119
    • Yao, S.1    Howlett, G.J.2    Norton, R.S.3
  • 10
    • 24744440425 scopus 로고    scopus 로고
    • Diffusion NMR spectroscopy: folding and aggregation of domains in p53
    • Dehner A., and Kessler H. Diffusion NMR spectroscopy: folding and aggregation of domains in p53. Chembiochem. 6 (2005) 1550-1565
    • (2005) Chembiochem. , vol.6 , pp. 1550-1565
    • Dehner, A.1    Kessler, H.2
  • 11
    • 7444227835 scopus 로고    scopus 로고
    • Measuring ligand-protein binding using NMR diffusion experiments
    • Lucas L.H., and Larive C.K. Measuring ligand-protein binding using NMR diffusion experiments. Concepts Magn. Reson. Part A 20A (2004) 24-41
    • (2004) Concepts Magn. Reson. Part A , vol.20 A , pp. 24-41
    • Lucas, L.H.1    Larive, C.K.2
  • 12
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins D.K., Grimshaw S.B., Receveur V., Dobson C.M., Jones J.A., and Smith L.J. Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 38 (1999) 16424-16431
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 14
    • 0141725721 scopus 로고    scopus 로고
    • 15N relaxation study of the cold shock protein CspB at various solvent viscosities
    • 15N relaxation study of the cold shock protein CspB at various solvent viscosities. J. Biomol. NMR 27 (2003) 221-234
    • (2003) J. Biomol. NMR , vol.27 , pp. 221-234
    • Zeeb, M.1    Jacob, M.H.2    Schindler, T.3    Balbach, J.4
  • 15
    • 0000449031 scopus 로고
    • The measurement of diffusion using deuterium pulsed field gradient nuclear magnetic resonance
    • Callaghan P.T., Legros M.A., and Pinder D.N. The measurement of diffusion using deuterium pulsed field gradient nuclear magnetic resonance. J. Chem. Phys. 79 (1983) 6372-6381
    • (1983) J. Chem. Phys. , vol.79 , pp. 6372-6381
    • Callaghan, P.T.1    Legros, M.A.2    Pinder, D.N.3
  • 16
    • 44949277996 scopus 로고
    • A PFG NMR experiment for accurate diffusion and flow studies in the presence of eddy currents
    • Gibbs S.J., and Johnson C.S. A PFG NMR experiment for accurate diffusion and flow studies in the presence of eddy currents. J. Magn. Reson. 93 (1991) 395-402
    • (1991) J. Magn. Reson. , vol.93 , pp. 395-402
    • Gibbs, S.J.1    Johnson, C.S.2
  • 17
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., and Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2 (1992) 661-665
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 18
    • 0000857723 scopus 로고    scopus 로고
    • Characterisation of protein unfolding by NMR diffusion measurements
    • Jones J.A., Wilkins D.K., Smith L.J., and Dobson C.M. Characterisation of protein unfolding by NMR diffusion measurements. J. Biomol. NMR 10 (1997) 199-203
    • (1997) J. Biomol. NMR , vol.10 , pp. 199-203
    • Jones, J.A.1    Wilkins, D.K.2    Smith, L.J.3    Dobson, C.M.4
  • 20
    • 33646733227 scopus 로고    scopus 로고
    • Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase
    • Bullock A.N., Debreczeni J.E., Edwards A.M., Sundstrom M., and Knapp S. Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 7637-7642
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 7637-7642
    • Bullock, A.N.1    Debreczeni, J.E.2    Edwards, A.M.3    Sundstrom, M.4    Knapp, S.5
  • 21
    • 0034328380 scopus 로고    scopus 로고
    • HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations
    • Garcia de la Torre J., Huertas M.L., and Carrasco B. 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
    • Garcia de la Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 23
    • 0001750817 scopus 로고    scopus 로고
    • Determination of oligomeric state of proteins in solution from pulsed-field-gradient self-diffusion coefficient measurements. A comparison of experimental, theoretical, and hard-sphere approximated values
    • Krishnan V.V. Determination of oligomeric state of proteins in solution from pulsed-field-gradient self-diffusion coefficient measurements. A comparison of experimental, theoretical, and hard-sphere approximated values. J. Magn. Reson. 124 (1997) 468-473
    • (1997) J. Magn. Reson. , vol.124 , pp. 468-473
    • Krishnan, V.V.1
  • 24
    • 0031202856 scopus 로고    scopus 로고
    • Determination of protein rotational correlation time from NMR relaxation data at various solvent viscosities
    • Korzhnev D.M., Orekhov V.Y., and Arseniev A.S. Determination of protein rotational correlation time from NMR relaxation data at various solvent viscosities. J. Magn. Reson. 127 (1997) 184-191
    • (1997) J. Magn. Reson. , vol.127 , pp. 184-191
    • Korzhnev, D.M.1    Orekhov, V.Y.2    Arseniev, A.S.3
  • 25
    • 0035619669 scopus 로고    scopus 로고
    • DOSY studies of hydrogen bond association: tetramethylsilane as a reference compound for diffusion studies
    • Cabrita E.J., and Berger S. DOSY studies of hydrogen bond association: tetramethylsilane as a reference compound for diffusion studies. Magn. Reson. Chem. 39 (2001) S142-S148
    • (2001) Magn. Reson. Chem. , vol.39
    • Cabrita, E.J.1    Berger, S.2
  • 26
    • 33947588571 scopus 로고    scopus 로고
    • Molecular mass estimation by PFG NMR spectroscopy
    • Crutchfield C.A., and Harris D.J. Molecular mass estimation by PFG NMR spectroscopy. J. Magn. Reson. 185 (2007) 179-182
    • (2007) J. Magn. Reson. , vol.185 , pp. 179-182
    • Crutchfield, C.A.1    Harris, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.