메뉴 건너뛰기




Volumn 35, Issue 3, 1996, Pages 698-703

Proline pipe helix: Structure of the tus proline repeat determined by 1H NMR

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; MEMBRANE PROTEIN;

EID: 0030064442     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952419l     Document Type: Article
Times cited : (8)

References (19)
  • 1
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • Bax, A., & Davis, D. G. (1985) Practical aspects of two-dimensional transverse NOE spectroscopy, J. Magn. Reson. 63, 355-360.
    • (1985) J. Magn. Reson. , vol.63 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 2
    • 0028101938 scopus 로고
    • Biophysical characteristics of Tus, the replication arrest protein of Escherichia coli
    • Coskun-Ari, F. F., Skokotas, A., Moe, G. R., & Hill, T. M. (1994) Biophysical characteristics of Tus, the replication arrest protein of Escherichia coli, J. Biol. Chem. 269, 11379-11385.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11379-11385
    • Coskun-Ari, F.F.1    Skokotas, A.2    Moe, G.R.3    Hill, T.M.4
  • 4
    • 33845378943 scopus 로고
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy, J. Am. Chem. Soc. 107, 2820-2821.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2820-2821
    • Davis, D.G.1    Bax, A.2
  • 5
    • 0025904730 scopus 로고
    • Defining solution conformations of small linear peptides
    • Dyson, H. J., & Wright, P. E. (1991) Defining solution conformations of small linear peptides, Annu. Rev. Biophys. Biophys. Chem. 20, 519-538.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 519-538
    • Dyson, H.J.1    Wright, P.E.2
  • 6
    • 0026767458 scopus 로고
    • Equilibrium, kinetic and footprinting studies of the Tus-Ter protein-DNA interaction
    • Gottlieb, P. A., Wu, S., Zhang, X., Tecklenburg, M., Kuempel, P., & Hill, T. M. ( 1992) Equilibrium, kinetic and footprinting studies of the Tus-Ter protein-DNA interaction. J. Biol. Chem. 267, 7434-7443.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7434-7443
    • Gottlieb, P.A.1    Wu, S.2    Zhang, X.3    Tecklenburg, M.4    Kuempel, P.5    Hill, T.M.6
  • 7
    • 0345311136 scopus 로고
    • Practical aspects of the E.COSY technique. Measurement of scalar spin-spin coupling constants in peptides
    • Griesinger, G., Sorensen, O. W., & Ernst, R. R. (1987) Practical aspects of the E.COSY technique. Measurement of scalar spin-spin coupling constants in peptides, J. Magn. Reson. 75, 474-492.
    • (1987) J. Magn. Reson. , vol.75 , pp. 474-492
    • Griesinger, G.1    Sorensen, O.W.2    Ernst, R.R.3
  • 8
    • 0028027784 scopus 로고
    • Tus prevents overreplication of oriC plasmid DNA
    • Hiasa, H., & Marians, K. J. (1994) Tus prevents overreplication of oriC plasmid DNA, J. Biol. Chem. 269, 26959-26968.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26959-26968
    • Hiasa, H.1    Marians, K.J.2
  • 9
    • 0026794488 scopus 로고
    • Arrest of bacterial DNA replication
    • Hill, T. (1992) Arrest of bacterial DNA replication. Annu. Rev. Microbiol. 46, 603-633.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 603-633
    • Hill, T.1
  • 10
    • 33745356391 scopus 로고
    • Contact electron-spin coupling of nuclear magnetic moments
    • Karplus, M. (1959) Contact electron-spin coupling of nuclear magnetic moments, J. Phys. Chem. 30, 11-15.
    • (1959) J. Phys. Chem. , vol.30 , pp. 11-15
    • Karplus, M.1
  • 11
    • 0028598746 scopus 로고
    • CD and DNA binding studies of a proline repeat-containing segment of the replication arrest protein Tus
    • Nedved, M. L., Gottlieb, P. A., & Moe, G. R. (1994) CD and DNA binding studies of a proline repeat-containing segment of the replication arrest protein Tus, Nucleic Acids Res. 22, 5024-5030.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5024-5030
    • Nedved, M.L.1    Gottlieb, P.A.2    Moe, G.R.3
  • 12
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms
    • Nilges, M., Clore, G. M., & Gronenborn, A. M. (1988) Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms, FEBS Lett. 239, 129-135.
    • (1988) FEBS Lett. , vol.239 , pp. 129-135
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 14
    • 0028071803 scopus 로고
    • Isolation and characterization of mutants of Tus, the replication arrest protein of Escherichia coli
    • Skokotas, A., Wrobleski, M., & Hill, T. M. (1994) Isolation and characterization of mutants of Tus, the replication arrest protein of Escherichia coli, J. Biol. Chem. 269, 20446-20455.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20446-20455
    • Skokotas, A.1    Wrobleski, M.2    Hill, T.M.3
  • 15
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States, D. J., Haberkorn, R. A., & Ruben, D. J. (1982) A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants, J. Magn. Reson. 48, 286-292.
    • (1982) J. Magn. Reson. , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 16
    • 0028279006 scopus 로고
    • Importance of Environment in Determining Secondary Structure in Proteins
    • Waterhous, D. V., & Johnson, W. C., Jr. (1994) Importance of Environment in Determining Secondary Structure in Proteins, Biochemistry 33, 2121-2128.
    • (1994) Biochemistry , vol.33 , pp. 2121-2128
    • Waterhous, D.V.1    Johnson Jr., W.C.2
  • 19
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance
    • Wüthrich, K., Billeter, M., & Braun, W. (1983) Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance, J. Mol. Biol. 160, 949-961.
    • (1983) J. Mol. Biol. , vol.160 , pp. 949-961
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.