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Volumn 440, Issue 7088, 2006, Pages 1227-1230

Detecting transient intermediates in macromolecular binding by paramagnetic NMR

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; CONSTRAINT THEORY; DNA; NUCLEAR MAGNETIC RESONANCE; PARAMAGNETISM; RELAXATION PROCESSES;

EID: 33646356250     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature04673     Document Type: Article
Times cited : (332)

References (27)
  • 2
    • 19744381543 scopus 로고    scopus 로고
    • Enhancement of association rates by nonspecific binding to DNA and cell membranes
    • Zhou, H.-X. & Szabo, A. Enhancement of association rates by nonspecific binding to DNA and cell membranes. Phys. Rev. Lett. 93, 178101 (2004).
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 178101
    • Zhou, H.-X.1    Szabo, A.2
  • 3
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • von Hippel, P. H. & Berg, O. G. Facilitated target location in biological systems. J. Biol. Chem. 264, 675-678 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 675-678
    • Von Hippel, P.H.1    Berg, O.G.2
  • 4
    • 3042579602 scopus 로고    scopus 로고
    • How do site-specific DNA-binding proteins find their targets?
    • Halford, S. E. & Marko, J. F. How do site-specific DNA-binding proteins find their targets? Nucleic Acids Res. 32, 3040-3052 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3040-3052
    • Halford, S.E.1    Marko, J.F.2
  • 5
    • 0029873697 scopus 로고    scopus 로고
    • Rapid, electrostatically assisted association of proteins
    • Schreiber, G. & Fersht, A. R. Rapid, electrostatically assisted association of proteins. Nature Struct. Biol. 3, 427-431 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 427-431
    • Schreiber, G.1    Fersht, A.R.2
  • 6
    • 0032557503 scopus 로고    scopus 로고
    • Electrostatic enhancement of diffusion-controlled protein-protein association: Comparison of theory and experiment on barnase and barstar
    • Vijayakumar, M. et al. Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar. J. Mol. Biol. 278, 1015-1024 (1998).
    • (1998) J. Mol. Biol. , vol.278 , pp. 1015-1024
    • Vijayakumar, M.1
  • 8
    • 36149008265 scopus 로고
    • Relaxation processes in a system of two spins
    • Solomon, I. Relaxation processes in a system of two spins. Phys. Rev. 99, 559-565 (1955).
    • (1955) Phys. Rev. , vol.99 , pp. 559-565
    • Solomon, I.1
  • 9
    • 0042033050 scopus 로고
    • Proton relaxation times in paramagnetic solutions. Effects of election spin relaxation
    • Bloembergen, N. & Morgan, L. O. Proton relaxation times in paramagnetic solutions. Effects of election spin relaxation. J. Chem. Phys. 34, 842-850 (1961).
    • (1961) J. Chem. Phys. , vol.34 , pp. 842-850
    • Bloembergen, N.1    Morgan, L.O.2
  • 10
    • 2442433447 scopus 로고    scopus 로고
    • 1H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule
    • 1H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule. J. Am. Chem. Soc. 126, 5879-5896 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5879-5896
    • Iwahara, J.1    Schwieters, C.D.2    Clore, G.M.3
  • 12
    • 0037533875 scopus 로고    scopus 로고
    • EDTA-derivatized deoxythymidine as a tool for rapid determination of protein binding polarity to DNA by intermolecular paramagnetic relaxation enhancement
    • Iwahara, J., Anderson, D. E., Murphy, E. C. & Clore, G. M. EDTA-derivatized deoxythymidine as a tool for rapid determination of protein binding polarity to DNA by intermolecular paramagnetic relaxation enhancement. J. Am. Chem. Soc. 125, 6634-6635 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6634-6635
    • Iwahara, J.1    Anderson, D.E.2    Murphy, E.C.3    Clore, G.M.4
  • 13
    • 0028103855 scopus 로고
    • Homeodomain-DNA recognition
    • Gehring, W. J. et al. Homeodomain-DNA recognition. Cell 78, 211-223 (1994).
    • (1994) Cell , vol.78 , pp. 211-223
    • Gehring, W.J.1
  • 14
    • 0027787519 scopus 로고
    • Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex
    • Billeter, M. et al. Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex. J. Mol. Biol. 234, 1084-1093 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 1084-1093
    • Billeter, M.1
  • 15
    • 0031851485 scopus 로고    scopus 로고
    • Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex
    • Fraenkel, E. & Pabo, C. O. Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex. Nature Struct. Biol. 5, 692-697 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 692-697
    • Fraenkel, E.1    Pabo, C.O.2
  • 16
    • 0032879507 scopus 로고    scopus 로고
    • R-factor, free R and complete cross-validation for dipolar coupling refinement of NMR structures
    • Clore, G. M. & Garrett, D. S. R-factor, free R and complete cross-validation for dipolar coupling refinement of NMR structures. J. Am. Chem. Soc. 121, 9008-9012 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9008-9012
    • Clore, G.M.1    Garrett, D.S.2
  • 17
    • 31544448614 scopus 로고    scopus 로고
    • Direct observation of enhanced translocation of a homeodomain between DNA cognate sites by NMR exchange spectroscopy
    • Iwahara, J. & Clore, G. M. Direct observation of enhanced translocation of a homeodomain between DNA cognate sites by NMR exchange spectroscopy. J. Am. Chem. Soc. 128, 404-405 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 404-405
    • Iwahara, J.1    Clore, G.M.2
  • 19
    • 0027412087 scopus 로고
    • Nucleotides flanking a conserved TAAT core dictate the DNA binding specificity of three murine homeodomain proteins
    • Catron, K. M., Iler, N. & Abate, C. Nucleotides flanking a conserved TAAT core dictate the DNA binding specificity of three murine homeodomain proteins. Mol. Cell. Biol. 13, 2354-2365 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2354-2365
    • Catron, K.M.1    Iler, N.2    Abate, C.3
  • 20
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: Implications for nuclear architecture and gene expression
    • Misteli, T. Protein dynamics: implications for nuclear architecture and gene expression. Science 291, 843-847 (2001).
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 21
    • 0004238344 scopus 로고    scopus 로고
    • Oxford Univ. Press, Oxford
    • Lewin, B. Genes VII (Oxford Univ. Press, Oxford, 2000).
    • (2000) Genes VII
    • Lewin, B.1
  • 22
    • 0031585990 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels
    • Gillespie, J. R. & Shortle, D. Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels. J. Mol. Biol. 268, 158-169 (1997).
    • (1997) J. Mol. Biol. , vol.268 , pp. 158-169
    • Gillespie, J.R.1    Shortle, D.2
  • 23
    • 0037174538 scopus 로고    scopus 로고
    • Derivation of structura restraints using a thiol-reactive chelator
    • Dvoretsky, A., Gaponenko, V. & Rosevear, P. R. Derivation of structura restraints using a thiol-reactive chelator. FEBS Lett. 528, 189-192 (2002).
    • (2002) FEBS Lett. , vol.528 , pp. 189-192
    • Dvoretsky, A.1    Gaponenko, V.2    Rosevear, P.R.3
  • 25
    • 0035840960 scopus 로고    scopus 로고
    • Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy
    • Donaldson, L. W. et al. Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy. J. Am. Chem. Soc. 123, 9843-9847 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9843-9847
    • Donaldson, L.W.1
  • 27
    • 0010957050 scopus 로고
    • Reaction rates by nuclear magnetic resonance
    • McConnell, H. M. Reaction rates by nuclear magnetic resonance. J. Chem. Phys. 28, 430-431 (1958).
    • (1958) J. Chem. Phys. , vol.28 , pp. 430-431
    • McConnell, H.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.