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Volumn 45, Issue 1-2, 2009, Pages 207-216

Chemical exchange effects during refocusing pulses in constant-time CPMG relaxation dispersion experiments

Author keywords

CPMG; Dynamics; NMR; Off resonance error; Protein; Relaxation

Indexed keywords

ARTICLE; CONTROLLED STUDY; DATA ANALYSIS; DISPERSION; MATHEMATICAL ANALYSIS; MATHEMATICAL COMPUTING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PREDICTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; SYSTEMATIC ERROR; TIME;

EID: 69249206511     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-009-9344-9     Document Type: Article
Times cited : (19)

References (32)
  • 1
    • 0002260957 scopus 로고    scopus 로고
    • A method for simulation of NOESY, ROESY, and Off-resonance ROESY spectra
    • Allard P, Helgstrand M, Hard T (1997) A method for simulation of NOESY, ROESY, and Off-resonance ROESY spectra. J Magn Reson 129:19-29
    • (1997) J Magn Reson , vol.129 , pp. 19-29
    • Allard, P.1    Helgstrand, M.2    Hard, T.3
  • 2
    • 0001900963 scopus 로고    scopus 로고
    • The complete homogeneous master equation for a heteronuclear two-spin system in the basis of Cartesian product operators
    • Allard P, Helgstrand M, Hard T (1998) The complete homogeneous master equation for a heteronuclear two-spin system in the basis of Cartesian product operators. J Magn Reson 134:7-16
    • (1998) J Magn Reson , vol.134 , pp. 7-16
    • Allard, P.1    Helgstrand, M.2    Hard, T.3
  • 3
    • 21244440196 scopus 로고    scopus 로고
    • Conservation of mu s-ms enzyme motions in the apo- and substrate-mimicked state
    • Beach H, Cole R, Gill ML, Loria JP (2005) Conservation of mu s-ms enzyme motions in the apo- and substrate-mimicked state. J Am Chem Soc 127:9167-9176
    • (2005) J Am Chem Soc , vol.127 , pp. 9167-9176
    • Beach, H.1    Cole, R.2    Gill, M.L.3    Loria, J.P.4
  • 4
    • 33646557015 scopus 로고    scopus 로고
    • Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy
    • Brath U, Akke M, Yang D, Kay LE, Mulder FA (2006) Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy. J Am Chem Soc 128:5718-5727
    • (2006) J Am Chem Soc , vol.128 , pp. 5718-5727
    • Brath, U.1    Akke, M.2    Yang, D.3    Kay, L.E.4    Mulder, F.A.5
  • 5
    • 0002889918 scopus 로고
    • General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation
    • Carver JP, Richards RE (1972) General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation. J Magn Reson 6:89-105
    • (1972) J Magn Reson , vol.6 , pp. 89-105
    • Carver, J.P.1    Richards, R.E.2
  • 7
    • 0035743580 scopus 로고    scopus 로고
    • Determination of the rotational diffusion tensor of macromolecules in solution from nmr relaxation data with a combination of exact and approximate methods - Application to the determination of interdomain orientation in multidomain proteins
    • Ghose R, Fushman D, Cowburn D (2001) Determination of the rotational diffusion tensor of macromolecules in solution from nmr relaxation data with a combination of exact and approximate methods - application to the determination of interdomain orientation in multidomain proteins. J Magn Reson 149:204-217
    • (2001) J Magn Reson , vol.149 , pp. 204-217
    • Ghose, R.1    Fushman, D.2    Cowburn, D.3
  • 8
    • 35048898436 scopus 로고    scopus 로고
    • An exchange-free measure of 15N transverse relaxation: An NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchange
    • Hansen DF, Yang D, Feng H, Zhou Z, Wiesner S, Bai Y, Kay LE (2007) An exchange-free measure of 15N transverse relaxation: An NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchange. J Am Chem Soc 129:11468-11478
    • (2007) J Am Chem Soc , vol.129 , pp. 11468-11478
    • Hansen, D.F.1    Yang, D.2    Feng, H.3    Zhou, Z.4    Wiesner, S.5    Bai, Y.6    Kay, L.E.7
  • 9
    • 58549087565 scopus 로고    scopus 로고
    • Conformational exchange in pseudoazurin: Different kinds of microsecond to millisecond dynamics characterized by their pH and buffer dependence using 15N NMR relaxation
    • Hass MA, Vlasie MD, Ubbink M, Led JJ (2009) Conformational exchange in pseudoazurin: Different kinds of microsecond to millisecond dynamics characterized by their pH and buffer dependence using 15N NMR relaxation. Biochemistry 48:50-58
    • (2009) Biochemistry , vol.48 , pp. 50-58
    • Hass, M.A.1    Vlasie, M.D.2    Ubbink, M.3    Led, J.J.4
  • 10
    • 0037355721 scopus 로고    scopus 로고
    • Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach
    • Ishima R, Torchia DA (2003) Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach. J Biomol NMR 25:243-248
    • (2003) J Biomol NMR , vol.25 , pp. 243-248
    • Ishima, R.1    Torchia, D.A.2
  • 11
    • 33646130861 scopus 로고    scopus 로고
    • Accuracy of optimized chemical-exchange parameters derived by fitting CPMG R2 dispersion profiles when R2(0a) not = R2(0b)
    • Ishima R, Torchia DA (2006) Accuracy of optimized chemical-exchange parameters derived by fitting CPMG R2 dispersion profiles when R2(0a) not = R2(0b). J Biomol NMR 34:209-219
    • (2006) J Biomol NMR , vol.34 , pp. 209-219
    • Ishima, R.1    Torchia, D.A.2
  • 12
    • 2942592052 scopus 로고    scopus 로고
    • Multiple-quantum relaxation dispersion NMR spectroscopy probing
    • Korzhnev DM, Kloiber K, Kay LE (2004) Multiple-quantum relaxation dispersion NMR spectroscopy probing. J Am Chem Soc 126:7320-7329
    • (2004) J Am Chem Soc , vol.126 , pp. 7320-7329
    • Korzhnev, D.M.1    Kloiber, K.2    Kay, L.E.3
  • 14
    • 33645929731 scopus 로고    scopus 로고
    • Faithful estimation of dynamics parameters from CPMG relaxation dispersion measurements
    • Kovrigin EL, Kempf JG, Grey MJ, Loria JP (2006) Faithful estimation of dynamics parameters from CPMG relaxation dispersion measurements. J Magn Reson 180:83-104
    • (2006) J Magn Reson , vol.180 , pp. 83-104
    • Kovrigin, E.L.1    Kempf, J.G.2    Grey, M.J.3    Loria, J.P.4
  • 16
    • 39749145723 scopus 로고    scopus 로고
    • Accurately probing slow motions on millisecond timescales with a robust NMR relaxation experiment
    • Long D, Liu M, Yang D (2008) Accurately probing slow motions on millisecond timescales with a robust NMR relaxation experiment. J Am Chem Soc 130:2432-2433
    • (2008) J Am Chem Soc , vol.130 , pp. 2432-2433
    • Long, D.1    Liu, M.2    Yang, D.3
  • 17
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy
    • Loria JP, Rance M, Palmer AG (1999) A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J Am Chem Soc 121:2331-2332
    • (1999) J Am Chem Soc , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 18
    • 40549133186 scopus 로고    scopus 로고
    • Characterization of enzyme motions by solution NMR relaxation dispersion
    • Loria JP, Berlow RB, Watt ED (2008) Characterization of enzyme motions by solution NMR relaxation dispersion. Acc Chem Res 41:212-221
    • (2008) Acc Chem Res , vol.41 , pp. 212-221
    • Loria, J.P.1    Berlow, R.B.2    Watt, E.D.3
  • 19
    • 36849127400 scopus 로고
    • Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution - Order of the reaction with respect to solvent
    • Luz Z, Meiboom S (1963) Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution - order of the reaction with respect to solvent. J Chem Phys 39:366-370
    • (1963) J Chem Phys , vol.39 , pp. 366-370
    • Luz, Z.1    Meiboom, S.2
  • 20
    • 0010957050 scopus 로고
    • Reaction rates by nuclear magnetic resonance
    • McConnell HM (1958) Reaction rates by nuclear magnetic resonance. J Chem Phys 28:430-431
    • (1958) J Chem Phys , vol.28 , pp. 430-431
    • McConnell, H.M.1
  • 21
    • 0002899752 scopus 로고
    • Modified spin-echo method for measuring nuclear relaxation times
    • Meiboom S, Gill D (1958) Modified spin-echo method for measuring nuclear relaxation times. Rev Sci Instrm 29:688-691
    • (1958) Rev Sci Instrm , vol.29 , pp. 688-691
    • Meiboom, S.1    Gill, D.2
  • 22
    • 0037138654 scopus 로고    scopus 로고
    • Slow internal dynamics in proteins: Application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme
    • Mulder FA, Hon B, Mittermaier A, Dahlquist FW, Kay LE (2002) Slow internal dynamics in proteins: Application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme. J Am Chem Soc 124:1443-1451
    • (2002) J Am Chem Soc , vol.124 , pp. 1443-1451
    • Mulder, F.A.1    Hon, B.2    Mittermaier, A.3    Dahlquist, F.W.4    Kay, L.E.5
  • 23
    • 68049139377 scopus 로고    scopus 로고
    • Practical aspects of 15N CPMG transverse relaxation experiments for proteins in solution
    • Myint W, Gong Q, Ishima R (2009) Practical aspects of 15N CPMG transverse relaxation experiments for proteins in solution. Concepts Magn Reson 34A:63-75
    • (2009) Concepts Magn Reson , vol.34 A , pp. 63-75
    • Myint, W.1    Gong, Q.2    Ishima, R.3
  • 24
    • 33744908076 scopus 로고    scopus 로고
    • Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy
    • Palmer AG 3rd, Massi F (2006) Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy. Chem Rev 106:1700-1719
    • (2006) Chem Rev , vol.106 , pp. 1700-1719
    • Palmer III, A.G.1    Massi, F.2
  • 25
    • 0000698894 scopus 로고    scopus 로고
    • Systematic errors associated with the CPMG pulse sequence and their effect on motional analysis of biomolecules
    • Ross A, Czisch M, King GC (1997) Systematic errors associated with the CPMG pulse sequence and their effect on motional analysis of biomolecules. J Magn Reson 124:355-365
    • (1997) J Magn Reson , vol.124 , pp. 355-365
    • Ross, A.1    Czisch, M.2    King, G.C.3
  • 26
    • 0037120879 scopus 로고    scopus 로고
    • Reconstructing NMR spectra of "invisible" excited protein states using
    • Skrynnikov NR, Dahlquist FW, Kay LE (2002) Reconstructing NMR spectra of "invisible" excited protein states using. J Am Chem Soc 124:12352-12360
    • (2002) J Am Chem Soc , vol.124 , pp. 12352-12360
    • Skrynnikov, N.R.1    Dahlquist, F.W.2    Kay, L.E.3
  • 27
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • Sugase K, Dyson HJ, Wright PE (2007) Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 447:1021-1025
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 28
    • 0141988954 scopus 로고    scopus 로고
    • Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: Binding of an antithrombin peptide to human prothrombin
    • Tolkatchev D, Xu P, Ni F (2003) Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: Binding of an antithrombin peptide to human prothrombin. J Am Chem Soc 125:12432-12442
    • (2003) J Am Chem Soc , vol.125 , pp. 12432-12442
    • Tolkatchev, D.1    Xu, P.2    Ni, F.3
  • 30
    • 14644394262 scopus 로고    scopus 로고
    • Microsecond-to-millisecond conformational dynamics demarcate the GluR2
    • Valentine ER, Palmer AG 3rd (2005) Microsecond-to-millisecond conformational dynamics demarcate the GluR2. Biochemistry 44:3410-3417
    • (2005) Biochemistry , vol.44 , pp. 3410-3417
    • Valentine, E.R.1    Palmer III, A.G.2
  • 31
    • 0035695509 scopus 로고    scopus 로고
    • CPMG sequences with enhanced sensitivity to chemical exchange
    • Wang C, Grey MJ, Palmer AG 3rd (2001) CPMG sequences with enhanced sensitivity to chemical exchange. J Biomol NMR 21:361-366
    • (2001) J Biomol NMR , vol.21 , pp. 361-366
    • Wang, C.1    Grey, M.J.2    Palmer III, A.G.3
  • 32
    • 7544221415 scopus 로고    scopus 로고
    • A phase cycle scheme that significantly suppresses offset-dependent artifacts in the R2-CPMG 15N relaxation experiment
    • Yip GN, Zuiderweg ER (2004) A phase cycle scheme that significantly suppresses offset-dependent artifacts in the R2-CPMG 15N relaxation experiment. J Magn Reson 171:25-36
    • (2004) J Magn Reson , vol.171 , pp. 25-36
    • Yip, G.N.1    Zuiderweg, E.R.2


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