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Volumn 20, Issue 1, 2009, Pages 41-46

Probing protein conformations by in situ non-covalent fluorescence labeling

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CONFORMATIONS; ENERGY TRANSFER; FLUORESCENCE SPECTROSCOPY; LIGANDS; PROTEINS; SPECTROSCOPIC ANALYSIS;

EID: 61849173429     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc8002088     Document Type: Article
Times cited : (19)

References (34)
  • 2
    • 14844352643 scopus 로고    scopus 로고
    • Conformational substates of calmodulin revealed by single-pair fluorescence resonance energy transfer: Influence of solution conditions and oxidative modification
    • Slaughter, B. D., Unruh, J. R., Allen, M. W., Bieber Urbauer, R. J., and Johnson, C. K. (2005) Conformational substates of calmodulin revealed by single-pair fluorescence resonance energy transfer: influence of solution conditions and oxidative modification. Biochemistry 44, 3694-707.
    • (2005) Biochemistry , vol.44 , pp. 3694-3707
    • Slaughter, B.D.1    Unruh, J.R.2    Allen, M.W.3    Bieber Urbauer, R.J.4    Johnson, C.K.5
  • 3
    • 34547880034 scopus 로고    scopus 로고
    • Single-molecule chemistry and biology special feature: Single-molecule FRET reveals sugar- induced conformational dynamics in LacY
    • Majumdar, D. S., Smirnova, I., Kasho, V., Nir, E., Kong, X., Weiss, S., and Kaback, H. R. (2007) Single-molecule chemistry and biology special feature: single-molecule FRET reveals sugar- induced conformational dynamics in LacY. Proc. Natl. Acad. Sci. U.S.A. 104, 12640-5.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 12640-12645
    • Majumdar, D.S.1    Smirnova, I.2    Kasho, V.3    Nir, E.4    Kong, X.5    Weiss, S.6    Kaback, H.R.7
  • 4
    • 38149104520 scopus 로고    scopus 로고
    • Direct visualization of asymmetric adenine nucleotide-induced conformational changes in MutLα
    • Sacho, E. J., Kadyrov, F. A., Modrich, P., Kunkel, T. A., and Erie, D. A. (2008) Direct visualization of asymmetric adenine nucleotide-induced conformational changes in MutLα. Mol. Cell 29, 112-21.
    • (2008) Mol. Cell , vol.29 , pp. 112-121
    • Sacho, E.J.1    Kadyrov, F.A.2    Modrich, P.3    Kunkel, T.A.4    Erie, D.A.5
  • 6
    • 0033813064 scopus 로고    scopus 로고
    • Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy
    • Weiss, S. (2000) Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy. Nat. Struct. Biol. 7, 724-9.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 724-729
    • Weiss, S.1
  • 7
    • 0036669824 scopus 로고    scopus 로고
    • Measuring protein conformational changes by FRET/LRET
    • Heyduk, T. (2002) Measuring protein conformational changes by FRET/LRET. Curr. Opin. Biotechnol. 13, 292-6.
    • (2002) Curr. Opin. Biotechnol , vol.13 , pp. 292-296
    • Heyduk, T.1
  • 8
    • 33645990641 scopus 로고    scopus 로고
    • Bridging conformational dynamics and function using single-molecule spectroscopy
    • Myong, S., Stevens, B. C., and Ha, T. (2006) Bridging conformational dynamics and function using single-molecule spectroscopy. Structure 14, 633-43.
    • (2006) Structure , vol.14 , pp. 633-643
    • Myong, S.1    Stevens, B.C.2    Ha, T.3
  • 9
    • 33646937406 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of protein folding and conformational dynamics
    • Michalet, X., Weiss, S., and Jager, M. (2006) Single-molecule fluorescence studies of protein folding and conformational dynamics. Chem. Rev. 106, 1785-813.
    • (2006) Chem. Rev , vol.106 , pp. 1785-1813
    • Michalet, X.1    Weiss, S.2    Jager, M.3
  • 10
    • 0036737063 scopus 로고    scopus 로고
    • A general strategy for site-specific double labeling of globular proteins for kinetic FRET studies
    • Ratner, V., Kahana, E., Eichler, M., and Haas, E. (2002) A general strategy for site-specific double labeling of globular proteins for kinetic FRET studies. Bioconjugate Chem. 13, 1163-70.
    • (2002) Bioconjugate Chem , vol.13 , pp. 1163-1170
    • Ratner, V.1    Kahana, E.2    Eichler, M.3    Haas, E.4
  • 11
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. (1998) The green fluorescent protein. Annu. Rev. Biochem. 67, 509-44.
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 13
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • Keppler, A., Gendreizig, S., Gronemeyer, T., Pick, H., Vogel, H., and Johnsson, K. (2003) A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nat. Biotechnol. 21, 86-9.
    • (2003) Nat. Biotechnol , vol.21 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Gronemeyer, T.3    Pick, H.4    Vogel, H.5    Johnsson, K.6
  • 14
    • 18744401100 scopus 로고    scopus 로고
    • Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase
    • Chen, I., Howarth, M., Lin, W., and Ting, A. Y. (2005) Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase. Nat Methods 2, 99-104.
    • (2005) Nat Methods , vol.2 , pp. 99-104
    • Chen, I.1    Howarth, M.2    Lin, W.3    Ting, A.Y.4
  • 15
    • 13444261101 scopus 로고    scopus 로고
    • Selective chemical labeling of proteins in living cells
    • Miller, L. W., and Cornish, V. W. (2005) Selective chemical labeling of proteins in living cells. Curr. Opin. Chem. Biol. 9, 56-61.
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 56-61
    • Miller, L.W.1    Cornish, V.W.2
  • 16
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
    • Miyawaki, A., and Tsien, R. Y. (2000) Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein. Methods Enzymol. 327, 472-500.
    • (2000) Methods Enzymol , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 18
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B. A., Adams, S. R., and Tsien, R. Y. (1998) Specific covalent labeling of recombinant protein molecules inside live cells. Science 281, 269-72.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 20
    • 33644535814 scopus 로고    scopus 로고
    • Site-specific labeling of proteins for single-molecule FRET by combining chemical and enzymatic modification
    • Jager, M., Nir, E., and Weiss, S. (2006) Site-specific labeling of proteins for single-molecule FRET by combining chemical and enzymatic modification. Protein Sci. 15, 640-6.
    • (2006) Protein Sci , vol.15 , pp. 640-646
    • Jager, M.1    Nir, E.2    Weiss, S.3
  • 21
    • 33947500247 scopus 로고    scopus 로고
    • Johnsson, N., and Johnsson, K. (2007) Chemical tools for biomolecular imaging. ACS Chem. Biol. 2, 31-8.
    • Johnsson, N., and Johnsson, K. (2007) Chemical tools for biomolecular imaging. ACS Chem. Biol. 2, 31-8.
  • 22
    • 22944441978 scopus 로고    scopus 로고
    • High-affinity adaptors for switchable recognition of histidine-tagged proteins
    • Lata, S., Reichel, A., Brock, R., Tampé, R., and Piehler, J. (2005) High-affinity adaptors for switchable recognition of histidine-tagged proteins. J. Am. Chem. Soc. 127, 10205-15.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 10205-10215
    • Lata, S.1    Reichel, A.2    Brock, R.3    Tampé, R.4    Piehler, J.5
  • 23
    • 33644516580 scopus 로고    scopus 로고
    • Specific and stable fluorescence labeling of histidine-tagged proteins for dissecting multi-protein complex formation
    • Lata, S., Gavutis, M., Tampé, R., and Piehler, J. (2006) Specific and stable fluorescence labeling of histidine-tagged proteins for dissecting multi-protein complex formation. J. Am. Chem. Soc. 128, 2365-72.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 2365-2372
    • Lata, S.1    Gavutis, M.2    Tampé, R.3    Piehler, J.4
  • 25
    • 0037133529 scopus 로고    scopus 로고
    • The human interferon receptor: NMR-based modeling, mapping of the IFN-α 2 binding site, and observed ligand-induced tightening
    • Chill, J. H., Nivasch, R., Levy, R., Albeck, S., Schreiber, G., and Anglister, J. (2002) The human interferon receptor: NMR-based modeling, mapping of the IFN-α 2 binding site, and observed ligand-induced tightening. Biochemistry 41, 3575-85.
    • (2002) Biochemistry , vol.41 , pp. 3575-3585
    • Chill, J.H.1    Nivasch, R.2    Levy, R.3    Albeck, S.4    Schreiber, G.5    Anglister, J.6
  • 27
    • 33644522358 scopus 로고    scopus 로고
    • Inquiring into the differential action of interferons (IFNs): An IFN-{α}2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-{β}
    • Jaitin, D. A., Roisman, L. C., Jaks, E., Gavutis, M., Piehler, J., Van der Heyden, J., Uze, G., and Schreiber, G. (2006) Inquiring into the differential action of interferons (IFNs): an IFN-{α}2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-{β}. Mol. Cell. Biol. 26, 1888-97.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 1888-1897
    • Jaitin, D.A.1    Roisman, L.C.2    Jaks, E.3    Gavutis, M.4    Piehler, J.5    Van der Heyden, J.6    Uze, G.7    Schreiber, G.8
  • 28
    • 84868895005 scopus 로고    scopus 로고
    • Specific and stable fluorescence labeling of histidine-tagged proteins for dissecting multi-protein complex formation
    • in press
    • Lata, S., Gavutis, M., Tampé, R., and Piehler, J. (2005)Specific and stable fluorescence labeling of histidine-tagged proteins for dissecting multi-protein complex formation. J. Am. Chem. Soc. in press.
    • (2005) J. Am. Chem. Soc
    • Lata, S.1    Gavutis, M.2    Tampé, R.3    Piehler, J.4
  • 29
    • 4143062575 scopus 로고    scopus 로고
    • Ligand-induced assembling of the type I interferon receptor on supported lipid bilayers
    • Lamken, P., Lata, S., Gavutis, M., and Piehler, J. (2004) Ligand-induced assembling of the type I interferon receptor on supported lipid bilayers. J. Mol. Biol. 341, 303-18.
    • (2004) J. Mol. Biol , vol.341 , pp. 303-318
    • Lamken, P.1    Lata, S.2    Gavutis, M.3    Piehler, J.4
  • 30
    • 0035504906 scopus 로고    scopus 로고
    • Time-resolved confocal scanning device for ultrasensitive fluorescence detection
    • Böhmer, M., Pampaloni, F., Wahl, M., Rahn, H. J., Erdmann, R., and Enderlein, J. (2001) Time-resolved confocal scanning device for ultrasensitive fluorescence detection. Rev. Sci. Instrum. 72, 4145-4152.
    • (2001) Rev. Sci. Instrum , vol.72 , pp. 4145-4152
    • Böhmer, M.1    Pampaloni, F.2    Wahl, M.3    Rahn, H.J.4    Erdmann, R.5    Enderlein, J.6
  • 31
    • 0027317178 scopus 로고
    • Fluorescence correlation spectroscopy with high count rate and low background: Analysis of translational diffusion
    • Rigler, R., Mets, Ü., Widengren, Ü., and Kask, P. (1993) Fluorescence correlation spectroscopy with high count rate and low background: analysis of translational diffusion. Eur. Biophys. J. 22, 169-175.
    • (1993) Eur. Biophys. J , vol.22 , pp. 169-175
    • Rigler, R.1    Mets, U.2    Widengren, U.3    Kask, P.4
  • 32
    • 0037632418 scopus 로고    scopus 로고
    • The human type I interferon receptor. NMR structure reveals the molecular basis of ligand binding
    • Chill, J. H., Quadt, S. R., Levy, R., Schreiber, G., and Anglister, J. (2003) The human type I interferon receptor. NMR structure reveals the molecular basis of ligand binding. Structure (Cambridge, U.K.) 11, 791-802.
    • (2003) Structure (Cambridge, U.K.) , vol.11 , pp. 791-802
    • Chill, J.H.1    Quadt, S.R.2    Levy, R.3    Schreiber, G.4    Anglister, J.5
  • 34
    • 33751080784 scopus 로고    scopus 로고
    • Determination of the human type I interferon receptor binding site on human interferon-alpha2 by cross saturation and an NMR-based model of the complex
    • Quadt-Akabayov, S. R., Chill, J. H., Levy, R., Kessler, N., and Anglister, J. (2006) Determination of the human type I interferon receptor binding site on human interferon-alpha2 by cross saturation and an NMR-based model of the complex. Protein Sci. 15, 2656-68.
    • (2006) Protein Sci , vol.15 , pp. 2656-2668
    • Quadt-Akabayov, S.R.1    Chill, J.H.2    Levy, R.3    Kessler, N.4    Anglister, J.5


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