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Volumn 53, Issue 4, 2012, Pages 303-310

A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: An application to protein folding

Author keywords

Excited protein conformational states; Methyl groups; Protein folding; Saturation transfer; Slow chemical exchange

Indexed keywords

CARBON 13; METHYL GROUP; NITROGEN 15; PROTEIN; PROTEIN L; PROTEIN SH3; UNCLASSIFIED DRUG; CARBON; FYN PROTEIN, HUMAN; NITROGEN; PROTEIN KINASE FYN;

EID: 84865118861     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-012-9640-7     Document Type: Article
Times cited : (68)

References (26)
  • 1
    • 0021373065 scopus 로고
    • NMR studies of enzymatic rates in vitro and in vivo by magnetization transfer
    • 10.1017/S0033583500005266
    • JR Alger RG Shulman 1984 NMR studies of enzymatic rates in vitro and in vivo by magnetization transfer Q Rev Biophys 17 83 124 10.1017/S0033583500005266
    • (1984) Q Rev Biophys , vol.17 , pp. 83-124
    • Alger, J.R.1    Shulman, R.G.2
  • 2
    • 84859208815 scopus 로고    scopus 로고
    • Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R1rho: An application to αb crystallin
    • 10.1007/s10858-012-9617-6
    • AJ Baldwin LE Kay 2012 Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R1rho: an application to αB crystallin J Biomol NMR 53 1 12 10.1007/s10858-012-9617-6
    • (2012) J Biomol NMR , vol.53 , pp. 1-12
    • Baldwin, A.J.1    Kay, L.E.2
  • 3
    • 0018736213 scopus 로고
    • Nuclear magnetic resonance studies of the binding of trimethoprim to dihydrofolate reductase
    • DOI 10.1021/bi00585a008
    • PJ Cayley JP Albrand J Feeney GC Roberts EA Piper AS Burgen 1979 Nuclear magnetic resonance studies of the binding of trimethoprim to dihydrofolate reductase Biochemistry 18 3886 3895 10.1021/bi00585a008 (Pubitemid 10224106)
    • (1979) Biochemistry , vol.18 , Issue.18 , pp. 3886-3895
    • Cayley, P.J.1    Albrand, J.P.2    Feeney, J.3
  • 4
    • 83055176454 scopus 로고    scopus 로고
    • Atomic-resolution dynamics on the surface of amyloid-beta protofibrils probed by solution NMR
    • 2011Natur.480.268F 10.1038/nature10577
    • NL Fawzi J Ying R Ghirlando DA Torchia GM Clore 2011 Atomic-resolution dynamics on the surface of amyloid-beta protofibrils probed by solution NMR Nature 480 268 272 2011Natur.480..268F 10.1038/nature10577
    • (2011) Nature , vol.480 , pp. 268-272
    • Fawzi, N.L.1    Ying, J.2    Ghirlando, R.3    Torchia, D.A.4    Clore, G.M.5
  • 5
    • 33846851242 scopus 로고
    • Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance
    • 1963JChPh.39.2892F 10.1063/1.1734121
    • S Forsen RA Hoffman 1963 Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance J Chem Phys 39 2892 2901 1963JChPh..39.2892F 10.1063/1.1734121
    • (1963) J Chem Phys , vol.39 , pp. 2892-2901
    • Forsen, S.1    Hoffman, R.A.2
  • 8
    • 0032608454 scopus 로고    scopus 로고
    • 1 Field Inhomogeneity. Are the Biases Assumed in Heteronuclear Relaxation Experiments Usually Underestimated?
    • M Guenneugues P Berthault H Desvaux 1999 A method for determining B1 field inhomogeneity. Are the biases assumed in heteronuclear relaxation experiments usually underestimated? J Magn Reson 136 118 126 1999JMagR.136..118G 10.1006/jmre.1998.1590 (Pubitemid 129607254)
    • (1999) Journal of Magnetic Resonance , vol.136 , Issue.1 , pp. 118-126
    • Guenneugues, M.1    Berthault, P.2    Desvaux, H.3
  • 9
    • 0014954355 scopus 로고
    • Double nuclear magnetic resonance observation of electron exchange between ferri- and ferro-cytochrome c
    • 1970Sci.169.1204G 10.1126/science.169.3951.1204
    • RK Gupta AG Redfield 1970 Double nuclear magnetic resonance observation of electron exchange between ferri- and ferro-cytochrome c Science 169 1204 1206 1970Sci...169.1204G 10.1126/science.169.3951.1204
    • (1970) Science , vol.169 , pp. 1204-1206
    • Gupta, R.K.1    Redfield, A.G.2
  • 10
    • 1642416319 scopus 로고    scopus 로고
    • Probing Slow Dynamics in High Molecular Weight Proteins by Methyl-TROSY NMR Spectroscopy: Application to a 723-Residue Enzyme
    • DOI 10.1021/ja039587i
    • DM Korzhnev K Kloiber V Kanelis V Tugarinov LE Kay 2004 Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme J Am Chem Soc 126 3964 3973 10.1021/ja039587i (Pubitemid 38391889)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.12 , pp. 3964-3973
    • Korzhnev, D.M.1    Kloiber, K.2    Kanelis, V.3    Tugarinov, V.4    Kay, L.E.5
  • 11
    • 3242880292 scopus 로고    scopus 로고
    • Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR
    • DOI 10.1038/nature02655
    • DM Korzhnev X Salvatella M Vendruscolo AA Di Nardo AR Davidson CM Dobson LE Kay 2004 Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR Nature 430 586 590 2004Natur.430..586K 10.1038/nature02655 (Pubitemid 38998635)
    • (2004) Nature , vol.430 , Issue.6999 , pp. 586-590
    • Korzhnev, D.M.1    Salvatella, X.2    Vendruscolo, M.3    Di Nardo, A.A.4    Davidson, A.R.5    Dobson, C.M.6    Kay, L.E.7
  • 12
    • 27644432794 scopus 로고    scopus 로고
    • Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: An application to the folding of a Fyn SH3 domain mutant
    • DOI 10.1021/ja054550e
    • DM Korzhnev P Neudecker A Mittermaier VY Orekhov LE Kay 2005 Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant J Am Chem Soc 127 15602 15611 10.1021/ja054550e (Pubitemid 41572534)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.44 , pp. 15602-15611
    • Korzhnev, D.M.1    Neudecker, P.2    Mittermaier, A.3    Orekhov, V.Yu.4    Kay, L.E.5
  • 13
    • 80051700610 scopus 로고    scopus 로고
    • Using the water signal to detect invisible exchanging protons in the catalytic triad of a serine protease
    • 10.1007/s10858-011-9527-z
    • CB Lauzon P van Zijl JT Stivers 2011 Using the water signal to detect invisible exchanging protons in the catalytic triad of a serine protease J Biomol NMR 50 299 314 10.1007/s10858-011-9527-z
    • (2011) J Biomol NMR , vol.50 , pp. 299-314
    • Lauzon, C.B.1    Van Zijl, P.2    Stivers, J.T.3
  • 14
    • 0009623221 scopus 로고
    • Symmetrical composite pulse sequences for NMR population-inversion. 2. Compensation of resonance offset
    • MH Levitt 1982 Symmetrical composite pulse sequences for NMR population-inversion. 2. Compensation of resonance offset J Magn Reson 50 95 110
    • (1982) J Magn Reson , vol.50 , pp. 95-110
    • Levitt, M.H.1
  • 15
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • D Marion M Ikura R Tschudin A Bax 1989 Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins J Magn Reson 85 393 399
    • (1989) J Magn Reson , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 16
    • 0010957050 scopus 로고
    • Reaction rates by nuclear magnetic resonance
    • 1958JChPh.28.430M 10.1063/1.1744152
    • HM McConnell 1958 Reaction rates by nuclear magnetic resonance J Chem Phys 28 430 431 1958JChPh..28..430M 10.1063/1.1744152
    • (1958) J Chem Phys , vol.28 , pp. 430-431
    • McConnell, H.M.1
  • 17
    • 0034741616 scopus 로고    scopus 로고
    • χ1 torsion angle dynamics in proteins, from dipolar couplings
    • DOI 10.1021/ja010595d
    • A Mittermaier LE Kay 2001 Chi1 torsion angle dynamics in proteins from dipolar couplings J Am Chem Soc 123 6892 6903 10.1021/ja010595d (Pubitemid 32884551)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.28 , pp. 6892-6903
    • Mittermaier, A.1    Kay, L.E.2
  • 18
    • 28244494171 scopus 로고    scopus 로고
    • Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy
    • DOI 10.1021/bi051771o
    • A Mittermaier DM Korzhnev LE Kay 2005 Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy Biochemistry 44 15430 15436 10.1021/bi051771o (Pubitemid 41706125)
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15430-15436
    • Mittermaier, A.1    Korzhnev, D.M.2    Kay, L.E.3
  • 19
  • 20
    • 48749138583 scopus 로고
    • Product operator formalism for the description of NMR pulse experiments
    • 10.1016/0079-6565(84)80005-9
    • OW Sorensen GW Eich MH Levitt G Bodenhausen RR Ernst 1983 Product operator formalism for the description of NMR pulse experiments Prog NMR Spectrosc 16 163 192 10.1016/0079-6565(84)80005-9
    • (1983) Prog NMR Spectrosc , vol.16 , pp. 163-192
    • Sorensen, O.W.1    Eich, G.W.2    Levitt, M.H.3    Bodenhausen, G.4    Ernst, R.R.5
  • 21
    • 84862061967 scopus 로고    scopus 로고
    • Studying 'invisible' excited protein states in slow exchange with a major conformation
    • 10.1021/ja3001419
    • P Vallurupalli G Bouvignies LE Kay 2012 Studying 'invisible' excited protein states in slow exchange with a major conformation J Am Chem Soc 134 8148 8161 10.1021/ja3001419
    • (2012) J Am Chem Soc , vol.134 , pp. 8148-8161
    • Vallurupalli, P.1    Bouvignies, G.2    Kay, L.E.3
  • 22
    • 0001068660 scopus 로고
    • Transverse relaxation in heteronuclear coupled spin systems: AX, AX2, AX3
    • 1976JChPh.64.320V 10.1063/1.431924
    • RR Vold RL Vold 1976 Transverse relaxation in heteronuclear coupled spin systems: AX, AX2, AX3 AXY J Chem Phys 64 320 332 1976JChPh..64..320V 10.1063/1.431924
    • (1976) AXY J Chem Phys , vol.64 , pp. 320-332
    • Vold, R.R.1    Vold, R.L.2
  • 23
    • 0034145982 scopus 로고    scopus 로고
    • A new class of contrast agents for MRI based on proton chemical exchange dependent saturation transfer (CEST)
    • 2000JMagR.143.79W 10.1006/jmre.1999.1956
    • KM Ward AH Aletras RS Balaban 2000 A new class of contrast agents for MRI based on proton chemical exchange dependent saturation transfer (CEST) J Magn Reson 143 79 87 2000JMagR.143...79W 10.1006/jmre.1999.1956
    • (2000) J Magn Reson , vol.143 , pp. 79-87
    • Ward, K.M.1    Aletras, A.H.2    Balaban, R.S.3
  • 24
    • 85023511576 scopus 로고
    • Intramolecular dipolar relaxation in multispin systems
    • LG Werbelow DM Grant 1977 Intramolecular dipolar relaxation in multispin systems Adv Magn Reson 9 189 299
    • (1977) Adv Magn Reson , vol.9 , pp. 189-299
    • Werbelow, L.G.1    Grant, D.M.2
  • 25
    • 0029181728 scopus 로고
    • 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 10.1007/BF00227471
    • DS Wishart CG Bigam A Holm RS Hodges BD Sykes 1995 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects J Biomol NMR 5 67 81 10.1007/BF00227471
    • (1995) J Biomol NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 26
    • 33747238228 scopus 로고    scopus 로고
    • Chemical exchange saturation transfer imaging and spectroscopy
    • 10.1016/j.pnmrs.2006.01.001
    • JY Zhou PCM van Zijl 2006 Chemical exchange saturation transfer imaging and spectroscopy Prog Nucl Magn Reson Spectrosc 48 109 136 10.1016/j.pnmrs.2006. 01.001
    • (2006) Prog Nucl Magn Reson Spectrosc , vol.48 , pp. 109-136
    • Zhou, J.Y.1    Van Zijl, P.C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.