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Volumn 426, Issue 7, 2014, Pages 1554-1567

Evidence against the "y-T Coupling" Mechanism of activation in the response regulator NtrC

Author keywords

allostery; CheY; NMR spectroscopy; protein dynamics; two component systems

Indexed keywords

ADENOSINE TRIPHOSPHATASE; LEUCINE; NITROGEN REGULATORY PROTEIN C; REGULATOR PROTEIN; TYROSINE; UNCLASSIFIED DRUG; NITROGEN REGULATORY PROTEIN;

EID: 84895918624     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.12.027     Document Type: Article
Times cited : (28)

References (77)
  • 1
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • B.F. Volkman, D. Lipson, D.E. Wemmer, and D. Kern Two-state allosteric behavior in a single-domain signaling protein Science 291 2001 2429 2433
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 2
    • 71149087504 scopus 로고    scopus 로고
    • Transient non-native hydrogen bonds promote activation of a signaling protein
    • A.K. Gardino, J. Villali, A. Kivenson, M. Lei, C.F. Liu, and P. Steindel et al. Transient non-native hydrogen bonds promote activation of a signaling protein Cell 139 2009 1109 1118
    • (2009) Cell , vol.139 , pp. 1109-1118
    • Gardino, A.K.1    Villali, J.2    Kivenson, A.3    Lei, M.4    Liu, C.F.5    Steindel, P.6
  • 3
    • 0024040412 scopus 로고
    • Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: Roles of the conserved amino-terminal domain of NTRC
    • J. Keener, and S. Kustu Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: roles of the conserved amino-terminal domain of NTRC Proc Natl Acad Sci USA 85 1988 4976 4980
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4976-4980
    • Keener, J.1    Kustu, S.2
  • 4
    • 33744780177 scopus 로고    scopus 로고
    • The structural basis for regulated assembly and function of the transcriptional activator NtrC
    • S. De Carlo, B.Y. Chen, T.R. Hoover, E. Kondrashkina, E. Nogales, and B.T. Nixon The structural basis for regulated assembly and function of the transcriptional activator NtrC Genes Dev 20 2006 1485 1495
    • (2006) Genes Dev , vol.20 , pp. 1485-1495
    • De Carlo, S.1    Chen, B.Y.2    Hoover, T.R.3    Kondrashkina, E.4    Nogales, E.5    Nixon, B.T.6
  • 5
    • 0026070143 scopus 로고
    • The phosphorylated form of the enhancer-binding protein NtrC has an ATPase activity that is essential for activation of transcription
    • D.S. Weiss, J. Batut, K.E. Klose, J. Keener, and S. Kustu The phosphorylated form of the enhancer-binding protein NtrC has an ATPase activity that is essential for activation of transcription Cell 67 1991 155 167
    • (1991) Cell , vol.67 , pp. 155-167
    • Weiss, D.S.1    Batut, J.2    Klose, K.E.3    Keener, J.4    Kustu, S.5
  • 6
    • 0025035371 scopus 로고
    • DNA-looping and enhancer activity: Association between DNA-bound NtrC activator and RNA polymerase at the bacterial glnA promoter
    • W. Su, S. Porter, S. Kustu, and H. Echols DNA-looping and enhancer activity: association between DNA-bound NtrC activator and RNA polymerase at the bacterial glnA promoter Proc Natl Acad Sci USA 87 1990 5504 5508
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5504-5508
    • Su, W.1    Porter, S.2    Kustu, S.3    Echols, H.4
  • 7
    • 0346220393 scopus 로고    scopus 로고
    • The role of dynamics in allosteric regulation
    • D. Kern, and E.R.P. Zuiderweg The role of dynamics in allosteric regulation Curr Opin Struct Biol 13 2003 748 757
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 748-757
    • Kern, D.1    Zuiderweg, E.R.P.2
  • 9
    • 0027366420 scopus 로고
    • Structural conservation in the CheY superfamily
    • K. Volz Structural conservation in the CheY superfamily Biochemistry 32 1993 11741 11753
    • (1993) Biochemistry , vol.32 , pp. 11741-11753
    • Volz, K.1
  • 10
    • 0025741662 scopus 로고
    • Crystal structure of Escherichia coli CheY refined at 1.7-Å resolution
    • K. Volz, and P. Matsumura Crystal structure of Escherichia coli CheY refined at 1.7-Å resolution J Biol Chem 266 1991 15511 15519
    • (1991) J Biol Chem , vol.266 , pp. 15511-15519
    • Volz, K.1    Matsumura, P.2
  • 11
    • 0035800848 scopus 로고    scopus 로고
    • A distinct meta-active conformation in the 1.1-angstrom resolution structure of wild-type apoCheY
    • M. Simonovic, and K. Volz A distinct meta-active conformation in the 1.1-angstrom resolution structure of wild-type apoCheY J Biol Chem 276 2001 28637 28640
    • (2001) J Biol Chem , vol.276 , pp. 28637-28640
    • Simonovic, M.1    Volz, K.2
  • 12
    • 0031058440 scopus 로고    scopus 로고
    • Crystal structures of CheY mutants Y106W and T871/Y106W: CheY activation correlates with movement of residue 106
    • X.Y. Zhu, J. Rebello, P. Matsumura, and K. Volz Crystal structures of CheY mutants Y106W and T871/Y106W: CheY activation correlates with movement of residue 106 J Biol Chem 272 1997 5000 5006
    • (1997) J Biol Chem , vol.272 , pp. 5000-5006
    • Zhu, X.Y.1    Rebello, J.2    Matsumura, P.3    Volz, K.4
  • 13
    • 33750435591 scopus 로고    scopus 로고
    • Switched or not?: The structure of unphosphorylated CheY bound to the N terminus of FliM
    • C.M. Dyer, and F.W. Dahlquist Switched or not?: the structure of unphosphorylated CheY bound to the N terminus of FliM J Bacteriol 188 2006 7354 7363
    • (2006) J Bacteriol , vol.188 , pp. 7354-7363
    • Dyer, C.M.1    Dahlquist, F.W.2
  • 14
    • 33750478377 scopus 로고    scopus 로고
    • A new perspective on response regulator activation
    • A.M. Stock, and J. Guhaniyogi A new perspective on response regulator activation J Bacteriol 188 2006 7328 7330
    • (2006) J Bacteriol , vol.188 , pp. 7328-7330
    • Stock, A.M.1    Guhaniyogi, J.2
  • 16
    • 37449018128 scopus 로고    scopus 로고
    • Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog
    • X.D. Zhao, D.M. Copeland, A.S. Soares, and A.H. West Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog J Mol Biol 375 2008 1141 1151
    • (2008) J Mol Biol , vol.375 , pp. 1141-1151
    • Zhao, X.D.1    Copeland, D.M.2    Soares, A.S.3    West, A.H.4
  • 17
    • 84871878701 scopus 로고    scopus 로고
    • The crystal structure of an activated Thermotoga maritima CheY with N-terminal region of FliM
    • D.R. Ahn, H. Song, J. Kim, S. Lee, and S. Park The crystal structure of an activated Thermotoga maritima CheY with N-terminal region of FliM Int J Biol Macromol 54 2013 76 83
    • (2013) Int J Biol Macromol , vol.54 , pp. 76-83
    • Ahn, D.R.1    Song, H.2    Kim, J.3    Lee, S.4    Park, S.5
  • 18
    • 84860445293 scopus 로고    scopus 로고
    • Crystal structure of receiver domain of putative NarL family response regulator spr1814 from Streptococcus pneumoniae in the absence and presence of the phosphoryl analog beryllofluoride
    • A.K. Park, J.H. Moon, K.S. Lee, and Y.M. Chi Crystal structure of receiver domain of putative NarL family response regulator spr1814 from Streptococcus pneumoniae in the absence and presence of the phosphoryl analog beryllofluoride Biochem Biophys Res Commun 421 2012 403 407
    • (2012) Biochem Biophys Res Commun , vol.421 , pp. 403-407
    • Park, A.K.1    Moon, J.H.2    Lee, K.S.3    Chi, Y.M.4
  • 19
    • 0042165841 scopus 로고    scopus 로고
    • High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain
    • C.A. Hastings, S.Y. Lee, H.S. Cho, D.L. Yan, S. Kustu, and D.E. Wemmer High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain Biochemistry 42 2003 9081 9090
    • (2003) Biochemistry , vol.42 , pp. 9081-9090
    • Hastings, C.A.1    Lee, S.Y.2    Cho, H.S.3    Yan, D.L.4    Kustu, S.5    Wemmer, D.E.6
  • 20
    • 33947619095 scopus 로고    scopus 로고
    • Insights into correlated motions and long-range interactions in CheY derived from molecular dynamics simulations
    • M.H. Knaggs, F.R. Salsbury, M.H. Edgell, and J.S. Fetrow Insights into correlated motions and long-range interactions in CheY derived from molecular dynamics simulations Biophys J 92 2007 2062 2079
    • (2007) Biophys J , vol.92 , pp. 2062-2079
    • Knaggs, M.H.1    Salsbury, F.R.2    Edgell, M.H.3    Fetrow, J.S.4
  • 21
    • 0036838326 scopus 로고    scopus 로고
    • Molecular dynamics of the FixJ receiver domain: Movement of the β4-α4 loop correlates with the in and out flip of Phe101
    • P. Roche, L. Mouawad, D. Perahia, J.P. Samama, and D. Kahn Molecular dynamics of the FixJ receiver domain: movement of the β4-α4 loop correlates with the in and out flip of Phe101 Protein Sci 11 2002 2622 2630
    • (2002) Protein Sci , vol.11 , pp. 2622-2630
    • Roche, P.1    Mouawad, L.2    Perahia, D.3    Samama, J.P.4    Kahn, D.5
  • 22
    • 79953293754 scopus 로고    scopus 로고
    • Statistical mechanics of protein allostery: Roles of backbone and side-chain structural fluctuations
    • K. Itoh, and M. Sasai Statistical mechanics of protein allostery: roles of backbone and side-chain structural fluctuations J Chem Phys 134 2011 125102
    • (2011) J Chem Phys , vol.134 , pp. 125102
    • Itoh, K.1    Sasai, M.2
  • 23
    • 50849120439 scopus 로고    scopus 로고
    • Coarse-grained dynamics of the receiver domain of NtrC: Fluctuations, correlations and implications for allosteric cooperativity
    • M.S. Liu, B.D. Todd, S.G. Yao, Z.P. Feng, R.S. Norton, and R.J. Sadus Coarse-grained dynamics of the receiver domain of NtrC: fluctuations, correlations and implications for allosteric cooperativity Proteins Struct Funct Bioinform 73 2008 218 227
    • (2008) Proteins Struct Funct Bioinform , vol.73 , pp. 218-227
    • Liu, M.S.1    Todd, B.D.2    Yao, S.G.3    Feng, Z.P.4    Norton, R.S.5    Sadus, R.J.6
  • 24
    • 84856514490 scopus 로고    scopus 로고
    • Detection of allosteric signal transmission by information-theoretic analysis of protein dynamics
    • A. Pandini, A. Fornili, F. Fraternali, and J. Kleinjung Detection of allosteric signal transmission by information-theoretic analysis of protein dynamics FASEB J 26 2012 868 881
    • (2012) FASEB J , vol.26 , pp. 868-881
    • Pandini, A.1    Fornili, A.2    Fraternali, F.3    Kleinjung, J.4
  • 25
    • 33646776723 scopus 로고    scopus 로고
    • Reconciling the "old" and "new" views of protein allostery: A molecular simulation study of chemotaxis y protein (CheY)
    • M.S. Formaneck, L. Ma, and Q. Cui Reconciling the "old" and "new" views of protein allostery: a molecular simulation study of chemotaxis Y protein (CheY) Proteins Struct Funct Bioinform 63 2006 846 867
    • (2006) Proteins Struct Funct Bioinform , vol.63 , pp. 846-867
    • Formaneck, M.S.1    Ma, L.2    Cui, Q.3
  • 26
    • 34548175177 scopus 로고    scopus 로고
    • Activation mechanism of a signaling protein at atomic resolution from advanced computations
    • L. Ma, and Q. Cui Activation mechanism of a signaling protein at atomic resolution from advanced computations J Am Chem Soc 129 2007 10261 10268
    • (2007) J Am Chem Soc , vol.129 , pp. 10261-10268
    • Ma, L.1    Cui, Q.2
  • 27
    • 84879088309 scopus 로고    scopus 로고
    • Colocalization of fast and slow timescale dynamics in the allosteric signaling protein CheY
    • L.R. McDonald, M.J. Whitley, J.A. Boyer, and A.L. Lee Colocalization of fast and slow timescale dynamics in the allosteric signaling protein CheY J Mol Biol 425 2013 2372 2381
    • (2013) J Mol Biol , vol.425 , pp. 2372-2381
    • McDonald, L.R.1    Whitley, M.J.2    Boyer, J.A.3    Lee, A.L.4
  • 28
    • 77949880884 scopus 로고    scopus 로고
    • Receiver domain structure and function in response regulator proteins
    • R.B. Bourret Receiver domain structure and function in response regulator proteins Curr Opin Microbiol 13 2010 142 149
    • (2010) Curr Opin Microbiol , vol.13 , pp. 142-149
    • Bourret, R.B.1
  • 29
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy
    • J.P. Loria, M. Rance, and A.G. Palmer A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy J Am Chem Soc 121 1999 2331 2332
    • (1999) J Am Chem Soc , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 31
    • 34250858152 scopus 로고    scopus 로고
    • Functional dynamics of response regulators using NMR relaxation techniques
    • A.K. Gardino, and D. Kern Functional dynamics of response regulators using NMR relaxation techniques Methods Enzymol 423 2007 149 167
    • (2007) Methods Enzymol , vol.423 , pp. 149-167
    • Gardino, A.K.1    Kern, D.2
  • 32
    • 40549133186 scopus 로고    scopus 로고
    • Characterization of enzyme motions by solution NMR relaxation dispersion
    • J.P. Loria, R.B. Berlow, and E.D. Watt Characterization of enzyme motions by solution NMR relaxation dispersion Acc Chem Res 41 2008 214 221
    • (2008) Acc Chem Res , vol.41 , pp. 214-221
    • Loria, J.P.1    Berlow, R.B.2    Watt, E.D.3
  • 33
    • 79958837339 scopus 로고    scopus 로고
    • An introduction to NMR-based approaches for measuring protein dynamics
    • I.R. Kleckner, and M.P. Foster An introduction to NMR-based approaches for measuring protein dynamics Biochim Biophys Acta Protein Proteomics 1814 2011 942 968
    • (2011) Biochim Biophys Acta Protein Proteomics , vol.1814 , pp. 942-968
    • Kleckner, I.R.1    Foster, M.P.2
  • 34
    • 84858292869 scopus 로고    scopus 로고
    • Multistate allostery in response regulators: Phosphorylation and mutagenesis activate RegA via alternate modes
    • B.S. Moorthy, and G.S. Anand Multistate allostery in response regulators: phosphorylation and mutagenesis activate RegA via alternate modes J Mol Biol 417 2012 468 487
    • (2012) J Mol Biol , vol.417 , pp. 468-487
    • Moorthy, B.S.1    Anand, G.S.2
  • 35
    • 0034624879 scopus 로고    scopus 로고
    • The 1.9 Å resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY
    • C.J. Halkides, M.M. McEvoy, E. Casper, P. Matsumura, K. Volz, and F.W. Dahlquist The 1.9 Å resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY Biochemistry 39 2000 5280 5286
    • (2000) Biochemistry , vol.39 , pp. 5280-5286
    • Halkides, C.J.1    McEvoy, M.M.2    Casper, E.3    Matsumura, P.4    Volz, K.5    Dahlquist, F.W.6
  • 36
    • 0030981418 scopus 로고    scopus 로고
    • Two-dimensional NMR methods for determining (chi 1) angles of aromatic residues in proteins from three-bond J(C'C gamma) and J(NC gamma) couplings
    • J.S. Hu, S. Grzesiek, and A. Bax Two-dimensional NMR methods for determining (chi 1) angles of aromatic residues in proteins from three-bond J(C'C gamma) and J(NC gamma) couplings J Am Chem Soc 119 1997 1803 1804
    • (1997) J Am Chem Soc , vol.119 , pp. 1803-1804
    • Hu, J.S.1    Grzesiek, S.2    Bax, A.3
  • 37
    • 77956478902 scopus 로고    scopus 로고
    • SPARTA plus: A modest improvement in empirical NMR chemical shift prediction by means of an artificial neural network
    • Y. Shen, and A. Bax SPARTA plus: a modest improvement in empirical NMR chemical shift prediction by means of an artificial neural network J Biomol NMR 48 2010 13 22
    • (2010) J Biomol NMR , vol.48 , pp. 13-22
    • Shen, Y.1    Bax, A.2
  • 38
    • 34249779857 scopus 로고    scopus 로고
    • Tyrosyl rotamer interconversion rates and the fluorescence decays of N-acetyltyrosinamide and short tyrosyl peptides
    • J.R. Unruh, M.R. Liyanage, and C.K. Johnson Tyrosyl rotamer interconversion rates and the fluorescence decays of N-acetyltyrosinamide and short tyrosyl peptides J Phys Chem B 111 2007 5494 5502
    • (2007) J Phys Chem B , vol.111 , pp. 5494-5502
    • Unruh, J.R.1    Liyanage, M.R.2    Johnson, C.K.3
  • 39
    • 0016433835 scopus 로고
    • NMR investigations of dynamics of aromatic amino-acid residues in basic pancreatic trypsin inhibitor
    • K. Wuthrich, and G. Wagner NMR investigations of dynamics of aromatic amino-acid residues in basic pancreatic trypsin inhibitor FEBS Lett 50 1975 265 268
    • (1975) FEBS Lett , vol.50 , pp. 265-268
    • Wuthrich, K.1    Wagner, G.2
  • 40
    • 0017335223 scopus 로고
    • 1H NMR studies at 360 MHz of aromatic amino acid residues in ferrocytorchrome C-552 from Euglena gracilis
    • 1H NMR studies at 360 MHz of aromatic amino acid residues in ferrocytorchrome C-552 from Euglena gracilis Biochim Biophys Acta 491 1977 416 422
    • (1977) Biochim Biophys Acta , vol.491 , pp. 416-422
    • Keller, R.M.1    Wuthrich, K.2
  • 41
    • 0035941549 scopus 로고    scopus 로고
    • Aromatic ring-flipping in supercooled water: Implications for NMR-based structural biology of proteins
    • J.J. Skalicky, J.L. Mills, S. Sharma, and T. Szyperski Aromatic ring-flipping in supercooled water: implications for NMR-based structural biology of proteins J Am Chem Soc 123 2001 388 397
    • (2001) J Am Chem Soc , vol.123 , pp. 388-397
    • Skalicky, J.J.1    Mills, J.L.2    Sharma, S.3    Szyperski, T.4
  • 42
    • 84879762225 scopus 로고    scopus 로고
    • 13C labeling strategy reveals a range of aromatic side chain motion in calmodulin
    • 13C labeling strategy reveals a range of aromatic side chain motion in calmodulin J Am Chem Soc 135 2013 9560 9563
    • (2013) J Am Chem Soc , vol.135 , pp. 9560-9563
    • Kasinath, V.1    Valentine, K.G.2    Wand, A.J.3
  • 43
    • 78651282059 scopus 로고    scopus 로고
    • P2CS: A database of prokaryotic two-component systems
    • M. Barakat, P. Ortet, and D.E. Whitworth P2CS: a database of prokaryotic two-component systems Nucleic Acids Res 39 2011 D771 D776
    • (2011) Nucleic Acids Res , vol.39
    • Barakat, M.1    Ortet, P.2    Whitworth, D.E.3
  • 44
    • 0033592861 scopus 로고    scopus 로고
    • Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators
    • D. Yan, H.S. Cho, C.A. Hastings, M.M. Igo, S.Y. Lee, and J.G. Pelton et al. Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators Proc Natl Acad Sci USA 96 1999 14789 14794
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14789-14794
    • Yan, D.1    Cho, H.S.2    Hastings, C.A.3    Igo, M.M.4    Lee, S.Y.5    Pelton, J.G.6
  • 45
    • 0029900040 scopus 로고    scopus 로고
    • Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coli
    • X.Y. Zhu, C.D. Amsler, K. Volz, and P. Matsumura Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coli J Bacteriol 178 1996 4208 4215
    • (1996) J Bacteriol , vol.178 , pp. 4208-4215
    • Zhu, X.Y.1    Amsler, C.D.2    Volz, K.3    Matsumura, P.4
  • 46
    • 4544243344 scopus 로고    scopus 로고
    • Structure of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide
    • C.M. Dyer, M.L. Quillin, A. Campos, J. Lu, M.M. McEnvoy, and A.C. Hausrath et al. Structure of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide J Mol Biol 39 2004 1325 1335
    • (2004) J Mol Biol , vol.39 , pp. 1325-1335
    • Dyer, C.M.1    Quillin, M.L.2    Campos, A.3    Lu, J.4    McEnvoy, M.M.5    Hausrath, A.C.6
  • 47
    • 0026583217 scopus 로고
    • Signal transduction and osmoregulation in Escherichia coli: A novel mutant of the positive regulator, OmpR, that functions in a phosphorylation- independent manner
    • K. Kanamaru, and T. Mizuno Signal transduction and osmoregulation in Escherichia coli: a novel mutant of the positive regulator, OmpR, that functions in a phosphorylation-independent manner J Biochem 111 1992 425 430
    • (1992) J Biochem , vol.111 , pp. 425-430
    • Kanamaru, K.1    Mizuno, T.2
  • 49
    • 33645834303 scopus 로고    scopus 로고
    • Review: New tools provide new insights in NMR studies of protein dynamics
    • A. Mittermaier, and L.E. Kay Review: new tools provide new insights in NMR studies of protein dynamics Science 312 2006 224 228
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 50
    • 0034984208 scopus 로고    scopus 로고
    • NMR probes of molecular dynamics: Overview and comparison with other techniques
    • A.G. Palmer NMR probes of molecular dynamics: overview and comparison with other techniques Annu Rev Biophys Biomol Struct 30 2001 129 155
    • (2001) Annu Rev Biophys Biomol Struct , vol.30 , pp. 129-155
    • Palmer, A.G.1
  • 51
    • 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
    • D.M. Korzhnev, P. Neudecker, A. Mittermaier, V.Y. Orekhov, and L.E. Kay 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 2005 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
  • 52
    • 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
    • M.J. Grey, C.Y. Wang, and A.G. Palmer Disulfide bond isomerization in basic pancreatic trypsin inhibitor: multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling J Am Chem Soc 125 2003 14324 14335
    • (2003) J Am Chem Soc , vol.125 , pp. 14324-14335
    • Grey, M.J.1    Wang, C.Y.2    Palmer, A.G.3
  • 53
    • 71449103005 scopus 로고    scopus 로고
    • Hidden alternative structures of proline isomerase essential for catalysis
    • J.S. Fraser, M.W. Clarkson, S.C. Degnan, R. Erion, D. Kern, and T. Alber Hidden alternative structures of proline isomerase essential for catalysis Nature 462 2009 669 673
    • (2009) Nature , vol.462 , pp. 669-673
    • Fraser, J.S.1    Clarkson, M.W.2    Degnan, S.C.3    Erion, R.4    Kern, D.5    Alber, T.6
  • 56
    • 35648945863 scopus 로고    scopus 로고
    • Phi-Value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy
    • P. Neudecker, A. Zarrine-Afsar, A.R. Davidson, and L.E. Kay phi-Value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy Proc Natl Acad Sci U S A 104 2007 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
  • 57
    • 84864830140 scopus 로고    scopus 로고
    • Segmental motions, not a two-state concerted switch, underlie allostery in CheY
    • L.R. McDonald, J.A. Boyer, and A.L. Lee Segmental motions, not a two-state concerted switch, underlie allostery in CheY Structure 20 2012 1363 1373
    • (2012) Structure , vol.20 , pp. 1363-1373
    • McDonald, L.R.1    Boyer, J.A.2    Lee, A.L.3
  • 58
    • 84860750796 scopus 로고    scopus 로고
    • Solution structure of a complex of the histidine autokinase CheA with its substrate CheY
    • G. Mo, H. Zhou, T. Kawamura, and F.W. Dahlquist Solution structure of a complex of the histidine autokinase CheA with its substrate CheY Biochemistry 51 2012 3786 3798
    • (2012) Biochemistry , vol.51 , pp. 3786-3798
    • Mo, G.1    Zhou, H.2    Kawamura, T.3    Dahlquist, F.W.4
  • 59
    • 0033603635 scopus 로고    scopus 로고
    • Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein FliM
    • M.M. McEvoy, A. Bren, M. Eisenbach, and F.W. Dahlquist Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein FliM J Mol Biol 289 1999 1423 1433
    • (1999) J Mol Biol , vol.289 , pp. 1423-1433
    • McEvoy, M.M.1    Bren, A.2    Eisenbach, M.3    Dahlquist, F.W.4
  • 61
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • A.G. Palmer, C.D. Kroenke, and J.P. Loria Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules Methods Enzymol 339 2001 204 238
    • (2001) Methods Enzymol , vol.339 , pp. 204-238
    • Palmer, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 63
  • 64
    • 0041866694 scopus 로고    scopus 로고
    • Mapping chemical exchange in proteins with MW > 50 kD
    • C.Y. Wang, M. Rance, and A.G. Palmer Mapping chemical exchange in proteins with MW > 50 kD J Am Chem Soc 125 2003 8968 8969
    • (2003) J Am Chem Soc , vol.125 , pp. 8968-8969
    • Wang, C.Y.1    Rance, M.2    Palmer, A.G.3
  • 66
    • 0033536573 scopus 로고    scopus 로고
    • Solution structure of the DNA-binding domain of NtrC with three alanine substitutions
    • J.G. Pelton, S. Kustu, and D.E. Wemmer Solution structure of the DNA-binding domain of NtrC with three alanine substitutions J Mol Biol 292 1999 1095 1110
    • (1999) J Mol Biol , vol.292 , pp. 1095-1110
    • Pelton, J.G.1    Kustu, S.2    Wemmer, D.E.3
  • 67
    • 0016631203 scopus 로고
    • Assay of inorganic and organic phosphorous in 0.1-5 nanomole range
    • H.H. Hess, and J.E. Derr Assay of inorganic and organic phosphorous in 0.1-5 nanomole range Anal Biochem 63 1975 607 613
    • (1975) Anal Biochem , vol.63 , pp. 607-613
    • Hess, H.H.1    Derr, J.E.2
  • 68
    • 69449087027 scopus 로고    scopus 로고
    • Segmented transition pathway of the signaling protein nitrogen regulatory protein C
    • M. Lei, J. Velos, A. Gardino, A. Kivenson, M. Karplus, and D. Kern Segmented transition pathway of the signaling protein nitrogen regulatory protein C J Mol Biol 392 2009 823 836
    • (2009) J Mol Biol , vol.392 , pp. 823-836
    • Lei, M.1    Velos, J.2    Gardino, A.3    Kivenson, A.4    Karplus, M.5    Kern, D.6
  • 70
    • 0242593434 scopus 로고    scopus 로고
    • Development and current status of the CHARMM force field for nucleic acids
    • A.D. MacKerell, N. Banavali, and N. Foloppe Development and current status of the CHARMM force field for nucleic acids Biopolymers 56 2001 257 265
    • (2001) Biopolymers , vol.56 , pp. 257-265
    • Mackerell, A.D.1    Banavali, N.2    Foloppe, N.3
  • 74
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • S.E. Feller, Y.H. Zhang, R.W. Pastor, and B.R. Brooks Constant pressure molecular dynamics simulation: the Langevin piston method J Chem Phys 103 1995 4613 4621
    • (1995) J Chem Phys , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.H.2    Pastor, R.W.3    Brooks, B.R.4
  • 75
    • 36449003554 scopus 로고
    • Constant pressure molecular dynamics algorithms
    • G.J. Martyna, D.J. Tobias, and M.L. Klein Constant pressure molecular dynamics algorithms J Chem Phys 101 1994 4177 4189
    • (1994) J Chem Phys , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3


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