메뉴 건너뛰기




Volumn 38, Issue 1, 2007, Pages 79-88

A single-quantum methyl 13C-relaxation dispersion experiment with improved sensitivity

Author keywords

Chemical exchange; CPMG; Methyl groups; Relaxation dispersion; Sensitivity enhancement

Indexed keywords

CARBON 13; PROTON;

EID: 34248530027     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-007-9149-7     Document Type: Article
Times cited : (107)

References (33)
  • 1
    • 0036407694 scopus 로고    scopus 로고
    • The structure of an FF domain from human HYPA/FBP11
    • Allen M, Friedler A, Schon O, Bycroft M (2002) The structure of an FF domain from human HYPA/FBP11. J Mol Biol 323:411-416
    • (2002) J Mol Biol , vol.323 , pp. 411-416
    • Allen, M.1    Friedler, A.2    Schon, O.3    Bycroft, M.4
  • 4
    • 0029882583 scopus 로고    scopus 로고
    • Access of ligands to cavities within the core of a protein is rapid
    • Feher VA, Baldwin EP, Dahlquist FW (1996) Access of ligands to cavities within the core of a protein is rapid. Nat Struct Biol 3:516-521
    • (1996) Nat Struct Biol , vol.3 , pp. 516-521
    • Feher, V.A.1    Baldwin, E.P.2    Dahlquist, F.W.3
  • 5
    • 44949280676 scopus 로고
    • Band-selective radiofrequency pulses
    • Geen H, Freeman R (1991) Band-selective radiofrequency pulses. J Magn Reson 93:93-141
    • (1991) J Magn Reson , vol.93 , pp. 93-141
    • Geen, H.1    Freeman, R.2
  • 6
    • 0032898682 scopus 로고    scopus 로고
    • A robust and costeffective method for the production of Val, Leu, Ile (δ1) methyl-protonated N-15-, C-13-, H-2-labeled proteins
    • Goto NK, Gardner KH, Mueller GA, Willis RC, Kay LE (1999) A robust and costeffective method for the production of Val, Leu, Ile (δ1) methyl-protonated N-15-, C-13-, H-2-labeled proteins. J Biomol NMR 13:369-374
    • (1999) J Biomol NMR , vol.13 , pp. 369-374
    • Goto, N.K.1    Gardner, K.H.2    Mueller, G.A.3    Willis, R.C.4    Kay, L.E.5
  • 7
    • 0029945313 scopus 로고    scopus 로고
    • Flexibility of DNA binding domain of trp repressor required for recognition of different operator sequences
    • Gryk MR, Jardetzky O, Klig LS, Yanofsky C (1996) Flexibility of DNA binding domain of trp repressor required for recognition of different operator sequences. Protein Sci 5:1195-1197
    • (1996) Protein Sci , vol.5 , pp. 1195-1197
    • Gryk, M.R.1    Jardetzky, O.2    Klig, L.S.3    Yanofsky, C.4
  • 8
    • 0034730994 scopus 로고    scopus 로고
    • Molecular motions and protein folding: Characterization of the backbone dynamics and folding equilibrium of αD-2 using C-13 NMR spin relaxation
    • Hill RB, Bracken C, DeGrado WF, Palmer AG (2000) Molecular motions and protein folding: Characterization of the backbone dynamics and folding equilibrium of αD-2 using C-13 NMR spin relaxation. J Am Chem Soc 122:11610-11619
    • (2000) J Am Chem Soc , vol.122 , pp. 11610-11619
    • Hill, R.B.1    Bracken, C.2    DeGrado, W.F.3    Palmer, A.G.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
    • 20444409471 scopus 로고    scopus 로고
    • The structure of the major transition state for folding of an FF domain from experiment and simulation
    • Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR (2005) The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol 350:363-378
    • (2005) J Mol Biol , vol.350 , pp. 363-378
    • Jemth, P.1    Day, R.2    Gianni, S.3    Khan, F.4    Allen, M.5    Daggett, V.6    Fersht, A.R.7
  • 13
    • 1642416319 scopus 로고    scopus 로고
    • Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: Application to a 723-residue enzyme
    • Korzhnev DM, Kloiber K, Kanelis V, Tugarinov V, Kay LE (2004a) 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
    • (2004) J Am Chem Soc , vol.126 , pp. 3964-3973
    • Korzhnev, D.M.1    Kloiber, K.2    Kanelis, V.3    Tugarinov, V.4    Kay, L.E.5
  • 14
    • 2942592052 scopus 로고    scopus 로고
    • Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: Theory and application
    • Korzhnev DM, Kloiber K, Kay LE (2004b) Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: Theory and application. 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
  • 16
    • 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
  • 17
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR-spectra without phase cycling - Application to the study of hydrogen-exchange in proteins
    • Marion D, Ikura M, Tschudin R, Bax A (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
  • 18
    • 0034728579 scopus 로고    scopus 로고
    • The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale
    • Millet O, Loria JP, Kroenke CD, Pons M, Palmer AG (2000) The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale. J Am Chem Soc 122:2867-2877
    • (2000) J Am Chem Soc , vol.122 , pp. 2867-2877
    • Millet, O.1    Loria, J.P.2    Kroenke, C.D.3    Pons, M.4    Palmer, A.G.5
  • 19
    • 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 FAA, 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.A.1    Hon, B.2    Mittermaier, A.3    Dahlquist, F.W.4    Kay, L.E.5
  • 21
    • 0035819455 scopus 로고    scopus 로고
    • Measurement of slow (μs-ms) time scale dynamics in protein side chains by N-15 relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme
    • Mulder FAA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE (2001b) Measurement of slow (μs-ms) time scale dynamics in protein side chains by N-15 relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme. J Am Chem Soc 123:967-975
    • (2001) J Am Chem Soc , vol.123 , pp. 967-975
    • Mulder, F.A.A.1    Skrynnikov, N.R.2    Hon, B.3    Dahlquist, F.W.4    Kay, L.E.5
  • 23
    • 0030217514 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of biopolymer dynamics
    • Palmer AG, Williams J, McDermott A (1996) Nuclear magnetic resonance studies of biopolymer dynamics. J Phys Chem 100:13293-13310
    • (1996) J Phys Chem , vol.100 , pp. 13293-13310
    • Palmer, A.G.1    Williams, J.2    McDermott, A.3
  • 24
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous solutions
    • Piotto M, Saudek V, Sklenar V (1992) Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous solutions. J Biomol NMR 2:661-665
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 27
    • 48749147783 scopus 로고
    • An improved sequence for broad band decoupling-WALTZ-16
    • Shaka AJ, Keeler J, Frenkiel T, Freeman R (1983) An improved sequence for broad band decoupling-WALTZ-16. J Magn Reson 52:335-338
    • (1983) J Magn Reson , vol.52 , pp. 335-338
    • Shaka, A.J.1    Keeler, J.2    Frenkiel, T.3    Freeman, R.4
  • 28
    • 0034809982 scopus 로고    scopus 로고
    • Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: Application to methionine residues in a cavity mutant of T4 lysozyme
    • Skrynnikov NR, Mulder FAA, Hon B, Dahlquist FW, Kay LE (2001) Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: Application to methionine residues in a cavity mutant of T4 lysozyme. J Am Chem Soc 123:4556-4566
    • (2001) J Am Chem Soc , vol.123 , pp. 4556-4566
    • Skrynnikov, N.R.1    Mulder, F.A.A.2    Hon, B.3    Dahlquist, F.W.4    Kay, L.E.5
  • 29
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • Sprangers R, Kay LE (2007) Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 445:718-722
    • (2007) Nature , vol.445 , pp. 718-722
    • Sprangers, R.1    Kay, L.E.2
  • 31
    • 0041930989 scopus 로고    scopus 로고
    • Cross-correlated relaxation enhanced H-1-C-13 NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes
    • Tugarinov V, Hwang PM, Ollerenshaw JE, Kay LE (2003) Cross-correlated relaxation enhanced H-1-C-13 NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. J Am Chem Soc 125:10420-10428
    • (2003) J Am Chem Soc , vol.125 , pp. 10420-10428
    • Tugarinov, V.1    Hwang, P.M.2    Ollerenshaw, J.E.3    Kay, L.E.4
  • 32
    • 33747049527 scopus 로고    scopus 로고
    • Complementarity of ensemble and single-molecule measures of protein motion: A relaxation dispersion NMR study of an enzyme complex
    • Vallurupalli P, Kay LE (2006) Complementarity of ensemble and single-molecule measures of protein motion: A relaxation dispersion NMR study of an enzyme complex. Proc Natl Acad Sci USA 103:11910-11915
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11910-11915
    • Vallurupalli, P.1    Kay, L.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.