메뉴 건너뛰기




Volumn 41, Issue 3, 2008, Pages 442-451

Probing invisible, low-populated states of protein molecules by relaxation dispersion NMR spectroscopy: An application to protein folding

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 42449102160     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar700189y     Document Type: Review
Times cited : (227)

References (33)
  • 1
    • 0028859279 scopus 로고
    • Protein modules and signaling networks
    • Pawson, T. Protein modules and signaling networks. Nature 1995, 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 5
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • Boehr, D. D.; McElheny, D.; Dyson, H. J.; Wright, P. E. The dynamic energy landscape of dihydrofolate reductase catalysis. Science 2006, 313, 1638-1642.
    • (2006) Science , vol.313 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wright, P.E.4
  • 7
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules
    • Palmer, A. G.; Kroenke, C. D.; Loria, J. P. Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol. 2001, 339, 204-238.
    • (2001) Methods Enzymol , vol.339 , pp. 204-238
    • Palmer, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 8
    • 0345306309 scopus 로고    scopus 로고
    • Disulfide bond isomerization in basic pancreatic trypsin inhibitor: Multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling
    • Grey, M. J.; Wang, C. Y.; Palmer, A. G. Disulfide bond isomerization in basic pancreatic trypsin inhibitor: Multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling. J. Am. Chem. Soc. 2003, 125, 14324-14335.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 14324-14335
    • Grey, M.J.1    Wang, C.Y.2    Palmer, A.G.3
  • 9
    • 0141988954 scopus 로고    scopus 로고
    • 15N NMR relaxation dispersion spectroscopy: Binding of an antithrombin peptide to human prothrombin
    • 15N NMR relaxation dispersion spectroscopy: Binding of an antithrombin peptide to human prothrombin. J. Am. Chem. Soc. 2003, 125, 12432-12442.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 12432-12442
    • Tolkatchev, D.1    Xu, P.2    Ni, F.3
  • 10
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy
    • Loria, J. P.; Rance, M.; Palmer, A. G. A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J. Am. Chem. Soc. 1999, 121, 2331-2332.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 11
    • 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, D. A. Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach. J. Biomol. NMR 2003, 25, 243-248.
    • (2003) J. Biomol. NMR , vol.25 , pp. 243-248
    • Ishima, R.1    Torchia, D.A.2
  • 12
    • 1242336825 scopus 로고    scopus 로고
    • Orekhov, V. Y.; Korzhnev, D. M.; Kay, L. E. Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in proteins. J. Am. Chem. Soc. 2004, 126, 1886-1891.
    • Orekhov, V. Y.; Korzhnev, D. M.; Kay, L. E. Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in proteins. J. Am. Chem. Soc. 2004, 126, 1886-1891.
  • 13
    • 2942592052 scopus 로고    scopus 로고
    • Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: Theory and application
    • Korzhnev, D. M.; Kloiber, K.; Kay, L. E. Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: Theory and application. J. Am. Chem. Soc. 2004, 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
    • 1842503159 scopus 로고    scopus 로고
    • Carbonyl carbon transverse relaxation dispersion measurements and ms-μs timescale motion in a protein hydrogen bond network
    • Ishima, R.; Baber, J.; Louis, J. M.; Torchia, D. A. Carbonyl carbon transverse relaxation dispersion measurements and ms-μs timescale motion in a protein hydrogen bond network. J. Biomol. NMR 2004, 29, 187-198.
    • (2004) J. Biomol. NMR , vol.29 , pp. 187-198
    • Ishima, R.1    Baber, J.2    Louis, J.M.3    Torchia, D.A.4
  • 15
    • 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, N. R.; Mulder, F. A. A.; Hon, B.; Dahlquist, F. W.; Kay, L. E. 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. 2001, 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
  • 16
    • 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, D. M.; Kloiber, K.; Kanelis, V.; Tugarinov, V.; Kay, L. E. Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: Application to a 723-residue enzyme. J. Am. Chem. Soc. 2004, 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
  • 17
    • 0035819455 scopus 로고    scopus 로고
    • Measurement of slow (μs-ms) time scale dynamics in protein side chains by 15N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme
    • Mulder, F. A. A.; Skrynnikov, N. R.; Hon, B.; Dahlquist, F. W.; Kay, L. E. Measurement of slow (μs-ms) time scale dynamics in protein side chains by 15N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme. J. Am. Chem. Soc. 2001, 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
  • 18
    • 33748675500 scopus 로고    scopus 로고
    • Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states
    • Korzhnev, D. M.; Neudecker, P.; Zarrine-Afsar, A.; Davidson, A. R.; Kay, L. E. Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states. Biochemistry 2006, 45, 10175-10183.
    • (2006) Biochemistry , vol.45 , pp. 10175-10183
    • Korzhnev, D.M.1    Neudecker, P.2    Zarrine-Afsar, A.3    Davidson, A.R.4    Kay, L.E.5
  • 19
    • 33750004434 scopus 로고    scopus 로고
    • Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopy
    • Neudecker, P.; Zarrine-Afsar, A.; Choy, W. Y.; Muhandiram, D. R.; Davidson, A. R.; Kay, L. E. Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopy. J. Mol. Biol. 2006, 363, 958-976.
    • (2006) J. Mol. Biol , vol.363 , pp. 958-976
    • Neudecker, P.1    Zarrine-Afsar, A.2    Choy, W.Y.3    Muhandiram, D.R.4    Davidson, A.R.5    Kay, L.E.6
  • 20
    • 33645954277 scopus 로고    scopus 로고
    • Hydration and packing along the folding pathway of a pair of SH3 domains by pressure dependent NMR
    • Bezsonova, I.; Korzhnev, D. M.; Prosser, R. S.; Forman-Kay, J. D.; Kay, L. E. Hydration and packing along the folding pathway of a pair of SH3 domains by pressure dependent NMR. Biochemistry 2006, 45, 4711-4719.
    • (2006) Biochemistry , vol.45 , pp. 4711-4719
    • Bezsonova, I.1    Korzhnev, D.M.2    Prosser, R.S.3    Forman-Kay, J.D.4    Kay, L.E.5
  • 22
    • 35648945863 scopus 로고    scopus 로고
    • Φ-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy
    • Neudecker, P.; Zarrine-Afsar, A.; Davidson, A. R.; Kay, L. E. Φ-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 15717-15722.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 15717-15722
    • Neudecker, P.1    Zarrine-Afsar, A.2    Davidson, A.R.3    Kay, L.E.4
  • 23
    • 28244494171 scopus 로고    scopus 로고
    • Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy
    • Mittermaier, A.; Korzhnev, D. M.; Kay, L. E. Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy. Biochemistry 2005, 44, 15430-15436.
    • (2005) Biochemistry , vol.44 , pp. 15430-15436
    • Mittermaier, A.1    Korzhnev, D.M.2    Kay, L.E.3
  • 27
    • 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
    • Korzhnev, D. M.; Neudecker, P.; Mittermaier, A.; Orekhov, V. Y.; Kay, L. E. 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. 2005, 127, 15602-15611.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 15602-15611
    • Korzhnev, D.M.1    Neudecker, P.2    Mittermaier, A.3    Orekhov, V.Y.4    Kay, L.E.5
  • 28
    • 0032007299 scopus 로고    scopus 로고
    • Kinetic studies of beta-sheet protein folding
    • Capaldi, A. P.; Radford, S. E. Kinetic studies of beta-sheet protein folding. Curr. Opin. Struct. Biol. 1998, 8, 86-92.
    • (1998) Curr. Opin. Struct. Biol , vol.8 , pp. 86-92
    • Capaldi, A.P.1    Radford, S.E.2
  • 30
    • 0036435907 scopus 로고    scopus 로고
    • Determination of a transition state at atomic resolution from protein engineering data
    • Paci, E.; Vendruscolo, M.; Dobson, C. M.; Karplus, M. Determination of a transition state at atomic resolution from protein engineering data. J. Mol. Biol. 2002, 324, 151-163.
    • (2002) J. Mol. Biol , vol.324 , pp. 151-163
    • Paci, E.1    Vendruscolo, M.2    Dobson, C.M.3    Karplus, M.4
  • 32
    • 2542599277 scopus 로고    scopus 로고
    • Φ-value analysis and the nature of protein-folding transition states
    • Fersht, A. R.; Sato, S. Φ-value analysis and the nature of protein-folding transition states. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 7976-7981.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 7976-7981
    • Fersht, A.R.1    Sato, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.