메뉴 건너뛰기




Volumn 347, Issue 2, 2005, Pages 297-307

Solution structure and dynamics of LuxU from Vibrio harveyi, a phosphotransferase protein involved in bacterial quorum sensing

Author keywords

Bioluminescence; LuxU; NMR; Quorum sensing; Solution structure

Indexed keywords

PHOSPHOTRANSFERASE; PROTEIN LUXU; UNCLASSIFIED DRUG;

EID: 14644388728     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.039     Document Type: Article
Times cited : (18)

References (68)
  • 2
    • 0009294561 scopus 로고
    • Identification of genes and gene products necessary for bacterial bioluminescence
    • J. Engebrecht, and M. Silverman Identification of genes and gene products necessary for bacterial bioluminescence Proc. Natl Acad. Sci. USA 81 1984 4154 4158
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 4154-4158
    • Engebrecht, J.1    Silverman, M.2
  • 4
    • 0033862847 scopus 로고    scopus 로고
    • Bacterial quorum sensing in pathogenic relationships
    • T.R. de Kievit, and B.H. Iglewski Bacterial quorum sensing in pathogenic relationships Infect. Immun. 68 2000 4839 4849
    • (2000) Infect. Immun. , vol.68 , pp. 4839-4849
    • De Kievit, T.R.1    Iglewski, B.H.2
  • 5
    • 0027412028 scopus 로고
    • Conjugation factor of Agrobacterium tumefaciens regulates Ti plasmid transfer by autoinduction
    • K.R. Piper, S. Beck von Bodman, and S.K. Farrand Conjugation factor of Agrobacterium tumefaciens regulates Ti plasmid transfer by autoinduction Nature 362 1993 448 450
    • (1993) Nature , vol.362 , pp. 448-450
    • Piper, K.R.1    Beck Von Bodman, S.2    Farrand, S.K.3
  • 6
    • 0003022471 scopus 로고
    • Intercellular communication in bioluminescence
    • J.A. Hoch T.J. Silhavy American Society for Microbiology Washington, DC
    • B.L. Bassler, and M.R. Silverman Intercellular communication in bioluminescence J.A. Hoch T.J. Silhavy Two-Component Signal Transduction 1994 American Society for Microbiology Washington, DC 431 445
    • (1994) Two-Component Signal Transduction , pp. 431-445
    • Bassler, B.L.1    Silverman, M.R.2
  • 7
    • 0027247722 scopus 로고
    • Intercellular signalling in Vibrio harveyi: Sequence and function of genes regulating expression of luminescence
    • B.L. Bassler, M. Wright, R.E. Showalter, and M.R. Silverman Intercellular signalling in Vibrio harveyi: sequence and function of genes regulating expression of luminescence Mol. Microbiol. 9 1993 773 786
    • (1993) Mol. Microbiol. , vol.9 , pp. 773-786
    • Bassler, B.L.1    Wright, M.2    Showalter, R.E.3    Silverman, M.R.4
  • 8
    • 0025964291 scopus 로고
    • Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay
    • D. Burbulys, K.A. Trach, and J.A. Hoch Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay Cell 64 1991 545 552
    • (1991) Cell , vol.64 , pp. 545-552
    • Burbulys, D.1    Trach, K.A.2    Hoch, J.A.3
  • 9
    • 0030595378 scopus 로고    scopus 로고
    • Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor
    • F. Posas, S.M. Wurgler-Murphy, T. Maeda, E.A. Witten, T.C. Thai, and H. Saito Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor Cell 86 1996 865 875
    • (1996) Cell , vol.86 , pp. 865-875
    • Posas, F.1    Wurgler-Murphy, S.M.2    Maeda, T.3    Witten, E.A.4    Thai, T.C.5    Saito, H.6
  • 10
    • 0030595328 scopus 로고    scopus 로고
    • Signal transduction via the multi-step phosphorelay: Not necessarily a road less traveled
    • J.L. Appleby, J.S. Parkinson, and R.B. Bourret Signal transduction via the multi-step phosphorelay: not necessarily a road less traveled Cell 86 1996 845 848
    • (1996) Cell , vol.86 , pp. 845-848
    • Appleby, J.L.1    Parkinson, J.S.2    Bourret, R.B.3
  • 11
    • 0343996104 scopus 로고
    • Sequences required for expression of Bordetella pertussis virulence factors share homology with prokaryotic signal transduction proteins
    • B. Arico, J.F. Miller, C. Roy, S. Stibitz, D. Monack, and S. Falkow Sequences required for expression of Bordetella pertussis virulence factors share homology with prokaryotic signal transduction proteins Proc. Natl Acad. Sci. USA 86 1989 6671 6675
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 6671-6675
    • Arico, B.1    Miller, J.F.2    Roy, C.3    Stibitz, S.4    Monack, D.5    Falkow, S.6
  • 12
    • 0025334736 scopus 로고
    • The arcB gene of Escherichia coli encodes a sensor-regulator protein for anaerobic repression of the arc modulon
    • S. Iuchi, Z. Matsuda, T. Fujiwara, and E.C. Lin The arcB gene of Escherichia coli encodes a sensor-regulator protein for anaerobic repression of the arc modulon Mol. Microbiol. 4 1990 715 727
    • (1990) Mol. Microbiol. , vol.4 , pp. 715-727
    • Iuchi, S.1    Matsuda, Z.2    Fujiwara, T.3    Lin, E.C.4
  • 13
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • J.A. Hoch Two-component and phosphorelay signal transduction Curr. Opin. Microbiol. 3 2000 165 170
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 14
    • 0028314003 scopus 로고
    • Deactivation of the sporulation transcription factor Spo0A by the Spo0E protein phosphatase
    • K.L. Ohlsen, J.K. Grimsley, and J.A. Hoch Deactivation of the sporulation transcription factor Spo0A by the Spo0E protein phosphatase Proc. Natl Acad. Sci. USA 91 1994 1756 1760
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1756-1760
    • Ohlsen, K.L.1    Grimsley, J.K.2    Hoch, J.A.3
  • 15
    • 0032927738 scopus 로고    scopus 로고
    • A genetic analysis of the function of LuxO, a two-component response regulator involved in quorum sensing in Vibrio harveyi
    • J.A. Freeman, and B.L. Bassler A genetic analysis of the function of LuxO, a two-component response regulator involved in quorum sensing in Vibrio harveyi Mol. Microbiol. 31 1999 665 677
    • (1999) Mol. Microbiol. , vol.31 , pp. 665-677
    • Freeman, J.A.1    Bassler, B.L.2
  • 16
    • 0024810911 scopus 로고
    • Purification and structural identification of an autoinducer for the luminescence system of Vibrio harveyi
    • J.G. Cao, and E.A. Meighen Purification and structural identification of an autoinducer for the luminescence system of Vibrio harveyi J. Biol. Chem. 264 1989 21670 21676
    • (1989) J. Biol. Chem. , vol.264 , pp. 21670-21676
    • Cao, J.G.1    Meighen, E.A.2
  • 18
    • 3142564584 scopus 로고    scopus 로고
    • The small RNA chaperone Hfq and multiple small RNAs control quorum sensing in Vibrio harveyi and Vibrio cholerae
    • D.H. Lenz, K.C. Mok, B.N. Lilley, R.V. Kulkarni, N.S. Wingreen, and B.L. Bassler The small RNA chaperone Hfq and multiple small RNAs control quorum sensing in Vibrio harveyi and Vibrio cholerae Cell 118 2004 69 82
    • (2004) Cell , vol.118 , pp. 69-82
    • Lenz, D.H.1    Mok, K.C.2    Lilley, B.N.3    Kulkarni, R.V.4    Wingreen, N.S.5    Bassler, B.L.6
  • 19
    • 0037450782 scopus 로고    scopus 로고
    • Vibrio harveyi quorum sensing: A coincidence detector for two autoinducers controls gene expression
    • K.C. Mok, N.S. Wingreen, and B.L. Bassler Vibrio harveyi quorum sensing: a coincidence detector for two autoinducers controls gene expression EMBO J. 22 2003 870 881
    • (2003) EMBO J. , vol.22 , pp. 870-881
    • Mok, K.C.1    Wingreen, N.S.2    Bassler, B.L.3
  • 20
    • 0032184886 scopus 로고    scopus 로고
    • Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase
    • K.I. Varughese, Madhusudan, X.Z. Zhou, J.M. Whiteley, and J.A. Hoch Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase Mol. Cell 2 1998 485 493
    • (1998) Mol. Cell , vol.2 , pp. 485-493
    • Varughese, K.I.1    Madhusudan2    Zhou, X.Z.3    Whiteley, J.M.4    Hoch, J.A.5
  • 21
    • 0344532884 scopus 로고    scopus 로고
    • Purification and preliminary crystallographic studies on the sporulation response regulatory phosphotransferase protein, Spo0B, from Bacillus subtilis
    • X.Z. Zhou, Madhusudan, J.M. Whiteley, J.A. Hoch, and K.I. Varughese Purification and preliminary crystallographic studies on the sporulation response regulatory phosphotransferase protein, Spo0B, from Bacillus subtilis Proteins: Struct. Funct. Genet. 27 1997 597 600
    • (1997) Proteins: Struct. Funct. Genet. , vol.27 , pp. 597-600
    • Zhou, X.Z.1    Madhusudan2    Whiteley, J.M.3    Hoch, J.A.4    Varughese, K.I.5
  • 22
    • 0030940479 scopus 로고    scopus 로고
    • Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB
    • M. Kato, T. Mizuno, T. Shimizu, and T. Hakoshima Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB Cell 88 1997 717 723
    • (1997) Cell , vol.88 , pp. 717-723
    • Kato, M.1    Mizuno, T.2    Shimizu, T.3    Hakoshima, T.4
  • 23
    • 0033536688 scopus 로고    scopus 로고
    • Conservation of structure and function among histidine-containing phosphotransfer (HPt) domains as revealed by the crystal structure of YPD1
    • Q. Xu, and A.H. West Conservation of structure and function among histidine-containing phosphotransfer (HPt) domains as revealed by the crystal structure of YPD1 J. Mol. Biol. 292 1999 1039 1050
    • (1999) J. Mol. Biol. , vol.292 , pp. 1039-1050
    • Xu, Q.1    West, A.H.2
  • 24
    • 0030813090 scopus 로고    scopus 로고
    • Molecular recognition in signal transduction: The interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis
    • Y.L. Tzeng, and J.A. Hoch Molecular recognition in signal transduction: the interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis J. Mol. Biol. 272 1997 200 212
    • (1997) J. Mol. Biol. , vol.272 , pp. 200-212
    • Tzeng, Y.L.1    Hoch, J.A.2
  • 25
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • M. Sattler, J. Schleucher, and C. Griesinger Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients Prog. NMR Spect. 34 1999 93 158
    • (1999) Prog. NMR Spect. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 26
    • 0024595889 scopus 로고
    • Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a
    • E. Zuiderweg, and S. Fesik Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a Biochemistry 28 1989 2387 2391
    • (1989) Biochemistry , vol.28 , pp. 2387-2391
    • Zuiderweg, E.1    Fesik, S.2
  • 28
    • 0025924784 scopus 로고
    • 13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: Application to interleukin 1β
    • 13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin 1β Biochemistry 30 1991 12 18
    • (1991) Biochemistry , vol.30 , pp. 12-18
    • Clore, G.M.1    Kay, L.E.2    Bax, A.3    Gronenborn, A.M.4
  • 29
    • 3242807429 scopus 로고    scopus 로고
    • 1H, (15)N, and (13)C chemical shift assignments of the Vibrio harveyi histidine phosphotransferase protein LuxU
    • D.L. Ulrich, R. Thompson, B. Bassler, J. Cavanagh, and J.P. Loria 1H, (15)N, and (13)C chemical shift assignments of the Vibrio harveyi histidine phosphotransferase protein LuxU J. Biomol. NMR 29 2004 551 552
    • (2004) J. Biomol. NMR , vol.29 , pp. 551-552
    • Ulrich, D.L.1    Thompson, R.2    Bassler, B.3    Cavanagh, J.4    Loria, J.P.5
  • 30
    • 0347610773 scopus 로고
    • 13C nuclear magnetic resonance chemical shifts
    • 13C nuclear magnetic resonance chemical shifts J. Am. Chem. Soc. 113 1991 5490 5492
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 35
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
    • G. Cornilescu, J.L. Marquardt, M. Ottiger, and A. Bax Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase J. Am. Chem. Soc. 120 1998 6836 6837
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 36
  • 38
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 40
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • L. Holm, and C. Sander Protein structure comparison by alignment of distance matrices J. Mol. Biol. 233 1993 123 138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 42
    • 0035903179 scopus 로고    scopus 로고
    • Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis
    • L. Mourey, S. Da Re, J.D. Pedelacq, T. Tolstykh, C. Faurie, and V. Guillet Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis J. Biol. Chem. 276 2001 31074 31082
    • (2001) J. Biol. Chem. , vol.276 , pp. 31074-31082
    • Mourey, L.1    Da Re, S.2    Pedelacq, J.D.3    Tolstykh, T.4    Faurie, C.5    Guillet, V.6
  • 43
    • 0028849132 scopus 로고
    • NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: Assignments, secondary structure, general fold, and backbone dynamics
    • H. Zhou, D.F. Lowry, R.V. Swanson, M.I. Simon, and F.W. Dahlquist NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics Biochemistry 34 1995 13858 13870
    • (1995) Biochemistry , vol.34 , pp. 13858-13870
    • Zhou, H.1    Lowry, D.F.2    Swanson, R.V.3    Simon, M.I.4    Dahlquist, F.W.5
  • 44
    • 0028865333 scopus 로고
    • Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase
    • L.C. Pedersen, M.M. Benning, and H.M. Holden Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase Biochemistry 34 1995 13305 13311
    • (1995) Biochemistry , vol.34 , pp. 13305-13311
    • Pedersen, L.C.1    Benning, M.M.2    Holden, H.M.3
  • 45
    • 0034980641 scopus 로고    scopus 로고
    • Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase
    • A.P. Turnbull, J.B. Rafferty, S.E. Sedelnikova, A.R. Slabas, T.P. Schierer, and J.T. Kroon Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase Structure (Camb) 9 2001 347 353
    • (2001) Structure (Camb) , vol.9 , pp. 347-353
    • Turnbull, A.P.1    Rafferty, J.B.2    Sedelnikova, S.E.3    Slabas, A.R.4    Schierer, T.P.5    Kroon, J.T.6
  • 46
    • 0032917463 scopus 로고    scopus 로고
    • Sequence and function of LuxU: A two-component phosphorelay protein that regulates quorum sensing in Vibrio harveyi
    • J.A. Freeman, and B.L. Bassler Sequence and function of LuxU: a two-component phosphorelay protein that regulates quorum sensing in Vibrio harveyi J. Bacteriol. 181 1999 899 906
    • (1999) J. Bacteriol. , vol.181 , pp. 899-906
    • Freeman, J.A.1    Bassler, B.L.2
  • 47
    • 0027456412 scopus 로고
    • Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques
    • J.G. Pelton, D.A. Torchia, N.D. Meadow, and S. Roseman Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques Protein Sci. 2 1993 543 558
    • (1993) Protein Sci. , vol.2 , pp. 543-558
    • Pelton, J.G.1    Torchia, D.A.2    Meadow, N.D.3    Roseman, S.4
  • 48
    • 0344436666 scopus 로고    scopus 로고
    • The yeast YPD1/SLN1 complex: Insights into molecular recognition in two-component signaling systems
    • Q. Xu, S.W. Porter, and A.H. West The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems Structure (Camb) 11 2003 1569 1581
    • (2003) Structure (Camb) , vol.11 , pp. 1569-1581
    • Xu, Q.1    Porter, S.W.2    West, A.H.3
  • 49
    • 5144231590 scopus 로고    scopus 로고
    • Solution structure of the Escherichia coli YojN histidine- phosphotransferase domain and its interaction with cognate phosphoryl receiver domains
    • V.V. Rogov, F. Bernhard, F. Lohr, and V. Dotsch Solution structure of the Escherichia coli YojN histidine-phosphotransferase domain and its interaction with cognate phosphoryl receiver domains J. Mol. Biol. 343 2004 1035 1048
    • (2004) J. Mol. Biol. , vol.343 , pp. 1035-1048
    • Rogov, V.V.1    Bernhard, F.2    Lohr, F.3    Dotsch, V.4
  • 52
    • 0033941615 scopus 로고    scopus 로고
    • Functional roles of conserved amino acid residues surrounding the phosphorylatable histidine of the yeast phosphorelay protein YPD1
    • F. Janiak-Spens, and A.H. West Functional roles of conserved amino acid residues surrounding the phosphorylatable histidine of the yeast phosphorelay protein YPD1 Mol. Microbiol. 37 2000 136 144
    • (2000) Mol. Microbiol. , vol.37 , pp. 136-144
    • Janiak-Spens, F.1    West, A.H.2
  • 53
    • 0026767328 scopus 로고
    • Characterization of the protonation and hydrogen bonding state of the histidine residues in IIAmtl, a domain of the phosphoenolpyruvate- dependent mannitol-specific transport protein
    • A.A. Van Dijk, R.M. Scheek, K. Dijkstra, G.K. Wolters, and G.T. Robillard Characterization of the protonation and hydrogen bonding state of the histidine residues in IIAmtl, a domain of the phosphoenolpyruvate- dependent mannitol-specific transport protein Biochemistry 31 1992 9063 9072
    • (1992) Biochemistry , vol.31 , pp. 9063-9072
    • Van Dijk, A.A.1    Scheek, R.M.2    Dijkstra, K.3    Wolters, G.K.4    Robillard, G.T.5
  • 54
    • 0001489595 scopus 로고
    • Nitrogen-15 nuclear magnetic resonance spectroscopy. Effects of hydrogen bonding and protonation on nitrogen chemical shifts in imidazoles
    • I.I. Schuster, and J.D. Roberts Nitrogen-15 nuclear magnetic resonance spectroscopy. Effects of hydrogen bonding and protonation on nitrogen chemical shifts in imidazoles J. Org. Chem. 44 1979 3864 3867
    • (1979) J. Org. Chem. , vol.44 , pp. 3864-3867
    • Schuster, I.I.1    Roberts, J.D.2
  • 55
    • 0033985890 scopus 로고    scopus 로고
    • A genetic analysis of the functions of LuxN: A two-component hybrid sensor kinase that regulates quorum sensing in Vibrio harveyi
    • J.A. Freeman, B.N. Lilley, and B.L. Bassler A genetic analysis of the functions of LuxN: a two-component hybrid sensor kinase that regulates quorum sensing in Vibrio harveyi Mol. Microbiol. 35 2000 139 149
    • (2000) Mol. Microbiol. , vol.35 , pp. 139-149
    • Freeman, J.A.1    Lilley, B.N.2    Bassler, B.L.3
  • 56
    • 0031571127 scopus 로고    scopus 로고
    • Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin
    • P.A. Carr, H.P. Erickson, and A.G. Palmer Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin Structure 5 1997 949 959
    • (1997) Structure , vol.5 , pp. 949-959
    • Carr, P.A.1    Erickson, H.P.2    Palmer, A.G.3
  • 57
    • 0033566242 scopus 로고    scopus 로고
    • Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F
    • V.A. Feher, and J. Cavanagh Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F Nature 400 1999 289 293
    • (1999) Nature , vol.400 , pp. 289-293
    • Feher, V.A.1    Cavanagh, J.2
  • 58
  • 59
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • P. Guntert, C. Mumenthaler, and K. Wuthrich Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 271 1997 283 298
    • (1997) J. Mol. Biol. , vol.271 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 61
    • 0000041361 scopus 로고
    • A common sense approach to peak picking two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams
    • D.S. Garrett, R. Powers, A. Gronenborn, and G. Clore A common sense approach to peak picking two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams J. Magn. Reson. 95 1991 214 220
    • (1991) J. Magn. Reson. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.3    Clore, G.4
  • 62
    • 34249765651 scopus 로고
    • NMRView-a computer program for the visualization and analysis of NMR data
    • B.A. Johnson, and R.A. Blevins NMRView-a computer program for the visualization and analysis of NMR data J. Biomol. NMR 4 1994 603 614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 63
    • 0030621858 scopus 로고    scopus 로고
    • Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation
    • E.G. Stein, L.M. Rice, and A.T. Brunger Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation J. Magn. Reson. 124 1997 154 164
    • (1997) J. Magn. Reson. , vol.124 , pp. 154-164
    • Stein, E.G.1    Rice, L.M.2    Brunger, A.T.3
  • 64
    • 0034792548 scopus 로고    scopus 로고
    • Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: An application to maltose binding protein
    • W.Y. Choy, M. Tollinger, G.A. Mueller, and L.E. Kay Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: an application to maltose binding protein J. Biomol. NMR 21 2001 31 40
    • (2001) J. Biomol. NMR , vol.21 , pp. 31-40
    • Choy, W.Y.1    Tollinger, M.2    Mueller, G.A.3    Kay, L.E.4
  • 67
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55 (see also pages 29-32)
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 68
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for multiple sequence alignments
    • C. Notredame, D. Higgins, and J. Heringa T-Coffee: a novel method for multiple sequence alignments J. Mol. Biol. 302 2000 205 217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.2    Heringa, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.