메뉴 건너뛰기




Volumn 46, Issue 3, 2010, Pages 205-216

Measurement of signs of chemical shift differences between ground and excited protein states: A comparison between H(S/M)QC and R 1ρ methods

Author keywords

Chemical exchange; Chemical shift; CPMG; H(S M)QC; Off resonance spin lock; Relaxation dispersion

Indexed keywords

ACTIN BINDING PROTEIN; PROTEIN KINASE FYN;

EID: 77951666296     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-009-9394-z     Document Type: Article
Times cited : (22)

References (55)
  • 1
    • 68249156465 scopus 로고    scopus 로고
    • Measuring the signs of 1H(alpha) chemical shift differences between ground and excited protein states by off-resonance spin-lock R(1rho) NMR spectroscopy
    • 10.1021/ja904315m
    • R Auer P Neudecker DR Muhandiram P Lundstrom DF Hansen R Konrat LE Kay 2009 Measuring the signs of 1H(alpha) chemical shift differences between ground and excited protein states by off-resonance spin-lock R(1rho) NMR spectroscopy J Am Chem Soc 131 10832 10833 10.1021/ja904315m
    • (2009) J Am Chem Soc , vol.131 , pp. 10832-10833
    • Auer, R.1    Neudecker, P.2    Muhandiram, D.R.3    Lundstrom, P.4    Hansen, D.F.5    Konrat, R.6    Kay, L.E.7
  • 2
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • DOI 10.1126/science.1130258
    • DD Boehr D McElheny HJ Dyson PE Wright 2006 The dynamic energy landscape of dihydrofolate reductase catalysis Science 313 1638 1642 10.1126/science. 1130258 2006Sci...313.1638B (Pubitemid 44414038)
    • (2006) Science , vol.313 , Issue.5793 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wrightt, P.E.4
  • 3
    • 0000073926 scopus 로고
    • Measurement of proton relaxation rates in proteins
    • 10.1007/BF00212519
    • B Boulat G Bodenhausen 1993 Measurement of proton relaxation rates in proteins J Biomol NMR 3 335 348 10.1007/BF00212519
    • (1993) J Biomol NMR , vol.3 , pp. 335-348
    • Boulat, B.1    Bodenhausen, G.2
  • 4
    • 33847534249 scopus 로고
    • Effects of diffusion on free precession in nuclear magnetic resonance experiments
    • 10.1103/PhysRev.94.630 1954PhRv.94.630C
    • HY Carr EM Purcell 1954 Effects of diffusion on free precession in nuclear magnetic resonance experiments Phys Rev 54 630 638 10.1103/PhysRev.94. 630 1954PhRv...94..630C
    • (1954) Phys Rev , vol.54 , pp. 630-638
    • Carr, H.Y.1    Purcell, E.M.2
  • 5
    • 0001186190 scopus 로고    scopus 로고
    • Selective cross-polarization in solution state NMR
    • 10.1080/002689798166396
    • E Chiarparin P Pelupessy G Bodenhausen 1998 Selective cross-polarization in solution state NMR Mol Phys 95 767 769 10.1080/002689798166396
    • (1998) Mol Phys , vol.95 , pp. 767-769
    • Chiarparin, E.1    Pelupessy, P.2    Bodenhausen, G.3
  • 6
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • 10.1007/BF00197809
    • F Delaglio S Grzesiek GW Vuister G Zhu J Pfeifer A Bax 1995 NMRPipe: a multidimensional spectral processing system based on UNIX pipes J Biomol NMR 6 277 293 10.1007/BF00197809
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 7
    • 34447503697 scopus 로고    scopus 로고
    • Conformational entropy in molecular recognition by proteins
    • DOI 10.1038/nature05959, PII NATURE05959
    • KK Frederick MS Marlow KG Valentine AJ Wand 2007 Conformational entropy in molecular recognition by proteins Nature 448 325 329 10.1038/nature05959 2007Natur.448..325F (Pubitemid 47080342)
    • (2007) Nature , vol.448 , Issue.7151 , pp. 325-329
    • Frederick, K.K.1    Marlow, M.S.2    Valentine, K.G.3    Wand, A.J.4
  • 8
    • 0033794450 scopus 로고    scopus 로고
    • New developments in isotope labeling strategies for protein solution NMR spectroscopy
    • 10.1016/S0959-440X(00)00135-4
    • NK Goto LE Kay 2000 New developments in isotope labeling strategies for protein solution NMR spectroscopy Curr Opin Struct Biol 10 585 592 10.1016/S0959-440X(00)00135-4
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 585-592
    • Goto, N.K.1    Kay, L.E.2
  • 9
    • 44949262025 scopus 로고    scopus 로고
    • An improved 15N relaxation dispersion experiment for the measurement of millisecond time-scale dynamics in proteins
    • 10.1021/jp074793o
    • DF Hansen P Vallurupalli LE Kay 2008 An improved 15N relaxation dispersion experiment for the measurement of millisecond time-scale dynamics in proteins J Phys Chem B 112 5898 5904 10.1021/jp074793o
    • (2008) J Phys Chem B , vol.112 , pp. 5898-5904
    • Hansen, D.F.1    Vallurupalli, P.2    Kay, L.E.3
  • 10
    • 39749156063 scopus 로고    scopus 로고
    • Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: How well can we do?
    • DOI 10.1021/ja078337p
    • DF Hansen P Vallurupalli P Lundstrom P Neudecker LE Kay 2008 Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do? J Am Chem Soc 130 2667 2675 10.1021/ja078337p (Pubitemid 351304782)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.8 , pp. 2667-2675
    • Hansen, D.F.1    Vallurupalli, P.2    Lundstrom, P.3    Neudecker, P.4    Kay, L.E.5
  • 11
    • 67849097846 scopus 로고    scopus 로고
    • Extending the range of microsecond-to-millisecond chemical exchange detected in labeled and unlabeled nucleic acids by selective carbon R(1rho) NMR spectroscopy
    • 10.1021/ja8091399
    • AL Hansen EN Nikolova A Casiano-Negroni HM Al-Hashimi 2009 Extending the range of microsecond-to-millisecond chemical exchange detected in labeled and unlabeled nucleic acids by selective carbon R(1rho) NMR spectroscopy J Am Chem Soc 131 3818 3819 10.1021/ja8091399
    • (2009) J Am Chem Soc , vol.131 , pp. 3818-3819
    • Hansen, A.L.1    Nikolova, E.N.2    Casiano-Negroni, A.3    Al-Hashimi, H.M.4
  • 12
    • 34548548791 scopus 로고    scopus 로고
    • The biologically relevant targets and binding affinity requirements for the function of the yeast actin-binding protein 1 Src-homology 3 domain vary with genetic context
    • DOI 10.1534/genetics.106.070300
    • J Haynes B Garcia EJ Stollar A Rath BJ Andrews AR Davidson 2007 The biologically relevant targets and binding affinity requirements for the function of the yeast actin-binding protein 1 SRC-homology 3 domain vary with genetic context Genetics 176 193 208 10.1534/genetics.106.070300 (Pubitemid 350021019)
    • (2007) Genetics , vol.176 , Issue.1 , pp. 193-208
    • Haynes, J.1    Garcia, B.2    Stollar, E.J.3    Rath, A.4    Andrews, B.J.5    Davidson, A.R.6
  • 13
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • DOI 10.1038/nature06522, PII NATURE06522
    • K Henzler-Wildman D Kern 2007 Dynamic personalities of proteins Nature 450 964 972 10.1038/nature06522 2007Natur.450..964H (Pubitemid 350273626)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 14
    • 33646945580 scopus 로고    scopus 로고
    • Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution
    • DOI 10.1021/cr040422h
    • TI Igumenova KK Frederick AJ Wand 2006 Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution Chem Rev 106 1672 1699 10.1021/cr040422h (Pubitemid 43792776)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1672-1699
    • Igumenova, T.I.1    Frederick, K.K.2    Wand, A.J.3
  • 15
    • 0033819054 scopus 로고    scopus 로고
    • Protein dynamics from NMR
    • 10.1038/78963
    • R Ishima DA Torchia 2000 Protein dynamics from NMR Nat Struct Biol 7 740 743 10.1038/78963
    • (2000) Nat Struct Biol , vol.7 , pp. 740-743
    • Ishima, R.1    Torchia, D.A.2
  • 16
    • 0037355721 scopus 로고    scopus 로고
    • Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach
    • DOI 10.1023/A:1022851228405
    • R Ishima D Torchia 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 10.1023/A:1022851228405 (Pubitemid 36410588)
    • (2003) Journal of Biomolecular NMR , vol.25 , Issue.3 , pp. 243-248
    • Ishima, R.1    Torchia, D.A.2
  • 17
    • 1842503159 scopus 로고    scopus 로고
    • Carbonyl carbon transverse relaxation dispersion measurements and ms-μ s timescale motion in a protein hydrogen bond network
    • DOI 10.1023/B:JNMR.0000019249.50306.5d
    • R Ishima J Baber JM Louis DA Torchia 2004 Carbonyl carbon transverse relaxation dispersion measurements and ms-micros timescale motion in a protein hydrogen bond network J Biomol NMR 29 187 198 10.1023/B:JNMR.0000019249.50306.5d (Pubitemid 38444480)
    • (2004) Journal of Biomolecular NMR , vol.29 , Issue.2 , pp. 187-198
    • Ishima, R.1    Baber, J.2    Louis, J.M.3    Torchia, D.A.4
  • 18
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • 10.1007/BF00404272
    • BA Johnson RA Blevins 1994 NMRView: a computer program for the visualization and analysis of NMR data J Biomol NMR 4 603 614 10.1007/BF00404272
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 19
    • 33644774471 scopus 로고    scopus 로고
    • Optimal isotope labelling for NMR protein structure determinations
    • DOI 10.1038/nature04525, PII N04525
    • M Kainosho T Torizawa Y Iwashita T Terauchi A Mei Ono P Guntert 2006 Optimal isotope labelling for NMR protein structure determinations Nature 440 52 57 10.1038/nature04525 2006Natur.440...52K (Pubitemid 43336263)
    • (2006) Nature , vol.440 , Issue.7080 , pp. 52-57
    • Kainosho, M.1    Torizawa, T.2    Iwashita, Y.3    Terauchi, T.4    Mei Ono, A.5    Guntert, P.6
  • 21
    • 0038365085 scopus 로고    scopus 로고
    • 1ρ relaxation outside of the fast exchange limit: An experimental study of a cavity mutant of T4 lysozyme
    • DOI 10.1023/A:1023039902737
    • DM Korzhnev VY Orekhov FW Dahlquist LE Kay 2003 Off-resonance R1rho relaxation outside of the fast exchange limit: an experimental study of a cavity mutant of T4 lysozyme J Biomol NMR 26 39 48 10.1023/A:1023039902737 (Pubitemid 36553451)
    • (2003) Journal of Biomolecular NMR , vol.26 , Issue.1 , pp. 39-48
    • Korzhnev, D.M.1    Orekhov, V.Yu.2    Dahlquist, F.W.3    Kay, L.E.4
  • 22
    • 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 10.1038/nature02655 2004Natur.430..586K (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
  • 23
    • 12944278747 scopus 로고    scopus 로고
    • 1ρ NMR studies of exchange dynamics in proteins with low spin-lock fields: An application to a fyn SH3 domain
    • DOI 10.1021/ja0446855
    • DM Korzhnev VY Orekhov LE Kay 2005 Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain J Am Chem Soc 127 713 721 10.1021/ja0446855 (Pubitemid 40174397)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.2 , pp. 713-721
    • Korzhnev, D.M.1    Orekhov, V.Yu.2    Kay, L.E.3
  • 25
    • 0033518882 scopus 로고    scopus 로고
    • NMR relaxation order parameter analysis of the dynamics of protein side chains
    • DOI 10.1021/ja982988r
    • DM LeMaster 1999 NMR relaxation order parameter analysis of the dynamics of protein side chains J Am Chem Soc 121 1726 1742 10.1021/ja982988r (Pubitemid 29124531)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.8 , pp. 1726-1742
    • LeMaster, D.M.1
  • 26
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy [13]
    • DOI 10.1021/ja983961a
    • JP Loria M Rance AG Palmer 1999 A relaxation compensated CPMG sequence for characterizing chemical exchange J Am Chem Soc 121 2331 2332 10.1021/ja983961a (Pubitemid 29152458)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.10 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer III, A.G.3
  • 29
    • 51749099362 scopus 로고    scopus 로고
    • Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: Comparison between uniformly and selectively (13)C labeled samples
    • 10.1007/s10858-008-9260-4
    • P Lundstrom DF Hansen LE Kay 2008 Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively (13)C labeled samples J Biomol NMR 42 35 47 10.1007/s10858-008-9260-4
    • (2008) J Biomol NMR , vol.42 , pp. 35-47
    • Lundstrom, P.1    Hansen, D.F.2    Kay, L.E.3
  • 30
    • 67749143936 scopus 로고    scopus 로고
    • Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy
    • 10.1021/ja807796a
    • P Lundstrom DF Hansen P Vallurupalli LE Kay 2009 Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy J Am Chem Soc 131 1915 1926 10.1021/ja807796a
    • (2009) J Am Chem Soc , vol.131 , pp. 1915-1926
    • Lundstrom, P.1    Hansen, D.F.2    Vallurupalli, P.3    Kay, L.E.4
  • 31
    • 67649392285 scopus 로고    scopus 로고
    • Measuring 13Cb chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy
    • 10.1007/s10858-009-9321-3
    • P Lundstrom H Lin LE Kay 2009 Measuring 13Cb chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy J Biomol NMR 44 139 145 10.1007/s10858-009-9321-3
    • (2009) J Biomol NMR , vol.44 , pp. 139-145
    • Lundstrom, P.1    Lin, H.2    Kay, L.E.3
  • 33
    • 0002899752 scopus 로고
    • Modified spin-echo method for measuring nuclear magnetic relaxation times
    • 10.1063/1.1716296 1958RScI.29.688M
    • S Meiboom D Gill 1958 Modified spin-echo method for measuring nuclear magnetic relaxation times Rev Sci Instrum 29 688 691 10.1063/1.1716296 1958RScI...29..688M
    • (1958) Rev Sci Instrum , vol.29 , pp. 688-691
    • Meiboom, S.1    Gill, D.2
  • 34
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • 10.1126/science.1124964 2006Sci.312.224M
    • A Mittermaier LE Kay 2006 New tools provide new insights in NMR studies of protein dynamics Science 312 224 228 10.1126/science.1124964 2006Sci...312..224M
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 35
    • 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
    • DOI 10.1016/j.jmb.2006.08.047, PII S002228360601076X
    • P Neudecker A Zarrine-Afsar WY Choy DR Muhandiram AR Davidson LE Kay 2006 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 363 958 976 10.1016/j.jmb.2006.08. 047 (Pubitemid 44573226)
    • (2006) Journal of Molecular Biology , vol.363 , Issue.5 , 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
  • 36
    • 1242336825 scopus 로고    scopus 로고
    • Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in proteins
    • 10.1021/ja038620y
    • VY Orekhov DM Korzhnev LE Kay 2004 Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in proteins J Am Chem Soc 126 1886 1891 10.1021/ja038620y
    • (2004) J Am Chem Soc , vol.126 , pp. 1886-1891
    • Orekhov, V.Y.1    Korzhnev, D.M.2    Kay, L.E.3
  • 37
    • 0030217514 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of biopolymer dynamics
    • 10.1021/jp9606117
    • AG Palmer J Williams A McDermott 1996 Nuclear magnetic resonance studies of biopolymer dynamics J Phys Chem 100 13293 13310 10.1021/jp9606117
    • (1996) J Phys Chem , vol.100 , pp. 13293-13310
    • Palmer, A.G.1    Williams, J.2    McDermott, A.3
  • 38
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • DOI 10.1016/S0076-6879(01)39315-1
    • AG Palmer CD Kroenke JP Loria 2001 NMR methods for quantifying microsecond-to-millisecond motions in biological macromolecules Methods Enzymol 339 204 238 10.1016/S0076-6879(01)39315-1 (Pubitemid 32666562)
    • (2001) Methods in Enzymology , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 39
    • 16244365477 scopus 로고    scopus 로고
    • Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems
    • DOI 10.1016/S0076-6879(05)94018-4, Nuclear Magnetic Resonance of Biological Macromolecules
    • AG Palmer MJ Grey C Wang 2005 Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems Methods Enzymol 394 430 465 10.1016/S0076-6879(05)94018-4 (Pubitemid 40460927)
    • (2005) Methods in Enzymology , vol.394 , pp. 430-465
    • Palmer III, A.G.1    Grey, M.J.2    Wang, C.3
  • 40
    • 85037451646 scopus 로고    scopus 로고
    • Hartmann-Hahn polarization transfer in liquids: An ideal tool for selective experiments
    • 10.1002/(SICI)1099-0534(2000)12:3<103::AID-CMR1>3.0.CO;2-#
    • P Pelupessy E Chiarparin 2000 Hartmann-Hahn polarization transfer in liquids: an ideal tool for selective experiments Concepts Magn Reson 12 103 124 10.1002/(SICI)1099-0534(2000)12:3<103::AID-CMR1>3.0.CO;2-#
    • (2000) Concepts Magn Reson , vol.12 , pp. 103-124
    • Pelupessy, P.1    Chiarparin, E.2
  • 41
    • 0000660936 scopus 로고
    • Mapping of spectral density functions using heteronuclear NMR relaxation measurements
    • JW Peng G Wagner 1992 Mapping of spectral density functions using heteronuclear NMR relaxation measurements J Magn Reson 98 308 332
    • (1992) J Magn Reson , vol.98 , pp. 308-332
    • Peng, J.W.1    Wagner, G.2
  • 42
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • 10.1007/BF02192855
    • M Piotto V Saudek V Sklenar 1992 Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions J Biomol NMR 2 661 665 10.1007/BF02192855
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 44
  • 45
    • 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
    • DOI 10.1021/ja004179p
    • NR Skrynnikov FAA Mulder B Hon FW Dahlquist LE Kay 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 10.1021/ja004179p (Pubitemid 32923384)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.19 , pp. 4556-4566
    • Skrynnikov, N.R.1    Mulder, F.A.A.2    Hon, B.3    Dahlquist, F.W.4    Kay, L.E.5
  • 46
    • 0037120879 scopus 로고    scopus 로고
    • Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments
    • DOI 10.1021/ja0207089
    • NR Skrynnikov FW Dahlquist LE Kay 2002 Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments J Am Chem Soc 124 12352 12360 10.1021/ja0207089 (Pubitemid 35154900)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.41 , pp. 12352-12360
    • Skrynnikov, N.R.1    Dahlquist, F.W.2    Kay, L.E.3
  • 47
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • DOI 10.1038/nature05858, PII NATURE05858
    • K Sugase HJ Dyson PE Wright 2007 Mechanism of coupled folding and binding of an intrinsically disordered protein Nature 447 1021 1024 10.1038/nature05858 2007Natur.447.1021S (Pubitemid 46975749)
    • (2007) Nature , vol.447 , Issue.7147 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 49
    • 0036018262 scopus 로고    scopus 로고
    • R1rho relaxation outside of the fast-exchange limit
    • 10.1006/jmre.2001.2466 2002JMagR.154.157T
    • O Trott AG Palmer 3rd 2002 R1rho relaxation outside of the fast-exchange limit J Magn Reson 154 157 160 10.1006/jmre.2001.2466 2002JMagR.154..157T
    • (2002) J Magn Reson , vol.154 , pp. 157-160
    • Trott, O.1    Palmer III, A.G.2
  • 50
    • 1242308875 scopus 로고    scopus 로고
    • An isotope labeling strategy for methyl TROSY spectroscopy
    • DOI 10.1023/B:JNMR.0000013824.93994.1f
    • V Tugarinov LE Kay 2004 An isotope labeling strategy for methyl TROSY spectroscopy J Biomol NMR 28 165 172 10.1023/B:JNMR.0000013824.93994.1f (Pubitemid 38232795)
    • (2004) Journal of Biomolecular NMR , vol.28 , Issue.2 , pp. 165-172
    • Tugarinov, V.1    Kay, L.E.2
  • 52
    • 50149085281 scopus 로고    scopus 로고
    • Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy
    • 10.1073/pnas.0804221105 2008PNAS.10511766V
    • P Vallurupalli DF Hansen LE Kay 2008 Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy Proc Natl Acad Sci U S A 105 11766 11771 10.1073/pnas.0804221105 2008PNAS..10511766V
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11766-11771
    • Vallurupalli, P.1    Hansen, D.F.2    Kay, L.E.3
  • 53
    • 33645458195 scopus 로고    scopus 로고
    • CEESY: Characterizing the conformation of unobservable protein states
    • 10.1021/ja0568749
    • H van Ingen GW Vuister S Wijmenga M Tessari 2006 CEESY: characterizing the conformation of unobservable protein states J Am Chem Soc 128 3856 3857 10.1021/ja0568749
    • (2006) J Am Chem Soc , vol.128 , pp. 3856-3857
    • Van Ingen, H.1    Vuister, G.W.2    Wijmenga, S.3    Tessari, M.4
  • 55
    • 31944446215 scopus 로고    scopus 로고
    • Resolving the motional modes that code for RNA adaptation
    • DOI 10.1126/science.1119488
    • Q Zhang X Sun ED Watt HM Al-Hashimi 2006 Resolving the motional modes that code for RNA adaptation Science 311 653 656 10.1126/science.1119488 2006Sci...311..653Z (Pubitemid 43191308)
    • (2006) Science , vol.311 , Issue.5761 , pp. 653-656
    • Zhang, Q.1    Sun, X.2    Watt, E.D.3    Al-Hashimi, H.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.