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Fluorescence energy transfer indicates similar transient and equilibrium intermediates in staphylococcal nuclease folding
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Creating a dynamic picture of the sliding clamp during T4 DNA polymerase holoenzyme assembly by using fluorescence resonance energy transfer
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Trakselis M.A., Alley S.C., Abel-Santos E., Benkovic S.J. Creating a dynamic picture of the sliding clamp during T4 DNA polymerase holoenzyme assembly by using fluorescence resonance energy transfer. Proc Natl Acad Sci USA. 98:2001;8368-8375. This work is an excellent example of utilizing the real-time detection capability of FRET. Rapid kinetics of functional conformational changes in a protein were studied.
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Trakselis, M.A.1
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FRET analysis indicates that the two ATPase active sites of the P-glycoprotein multidrug transporter are closely associated
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Qu, Q.1
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A FRET-based sensor reveals large ATP hydrolysis-induced conformational changes and three distinct states of the molecular motor myosin
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Shih W.M., Gryczynski Z., Lakowicz J.R., Spudich J.A. A FRET-based sensor reveals large ATP hydrolysis-induced conformational changes and three distinct states of the molecular motor myosin. Cell. 102:2000;683-694.
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Shih, W.M.1
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Structural organization of bacterial RNA polymerase holoenzyme and the RNA polymerase-promoter open complex
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Mekler V., Korthhonjia E., Mukhopadhyay J., Knight J., Revyakin A., Kapanidis A.N., Niu W., Ebright Y.W., Levy R., Ebright R.H. Structural organization of bacterial RNA polymerase holoenzyme and the RNA polymerase-promoter open complex. Cell. 108:2002;599-614. This is by far the most extensive use of FRET to probe the conformation of a protein. Novel, creative labeling methodologies were used to prepare a large number of donor-acceptor-labeled derivatives of RNA polymerase, a multisubunit enzyme. Hundreds of distances were measured and distance constrained docking procedures were used to determine the architecture of this large protein in two states.
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Mekler, V.1
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Incorporation of azides into recombinants proteins for chemoselective modification by the Staudinger ligation
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Novel fluorescence labeling and high-throughput assay technologies for in vitro analysis of protein interactions
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Doi N., Takashima H., Kinjo M., Sakata K., Kawahashi Y., Oishi Y., Oyama R., Miyamoto-Sato E., Sawasaki T., Endo Y., Yanagawa H. Novel fluorescence labeling and high-throughput assay technologies for in vitro analysis of protein interactions. Genome Res. 12:2002;487-492. A general and very flexible methodology for incorporating fluorescence labels into the C terminus of in vitro synthesized protein is described.
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Single-molecule protein folding: Diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2
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Deniz A.A., Laurence T.A., Beligere G.S., Dahan M., Martin A.B., Chemla D.S., Dawson P.E., Schultz P.G., Weiss S. Single-molecule protein folding: diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2. Proc Natl Acad Sci USA. 97:2000;5179-5184. The first study by FRET of a conformational change in a freely diffusing single protein molecule. Additionally, this paper illustrates nicely the potential of creating donor-acceptor labeled proteins using native protein ligation of fragments.
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Deniz, A.A.1
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Generation of a dual-labeled fluorescence biosensor for Crk-II phosphorylation using solid-phase expressed protein ligation
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Fluorescent monitoring of kinase activity in real time: Development of a robust fluorescence-based assay for Abl tyrosine kinase activity
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Luminescence energy transfer using a terbium chelate: Improvements on fluorescence energy transfer
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Luminescence energy transfer with lanthanide chelates: Interpretation of sensitized acceptor decay amplitudes
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Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy
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Cha A., Snyder G.E., Selvin P.R., Bezanilla F. Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy. Nature. 402:1999;809-813.
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27
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0036469062
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A role for interaction of the RNA polymerase flap domain with the σ subunit in promoter recognition
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Kuznedelov K., Minakhin L., Niedziela-Majka A., Dove S.L., Rogulja D., Nickels B.E., Hochschild A., Heyduk T., Severinov K. A role for interaction of the RNA polymerase flap domain with the σ subunit in promoter recognition. Science. 295:2002;855-857. A good example of the advantages of using LRET for studying intramolecular energy transfer. The combination of LRET with other biochemical experiments identified a 'molecular switch' responsible for a functional domain movement in RNA polymerase.
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Kuznedelov, K.1
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The use of site-directed fluorophore labeling and donor-donor energy migration to investigate solution structure and dynamics in proteins
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Conformational studies of plasminogen activator inhibitor type 1 by fluorescence spectroscopy. Analysis of the reactive center of inhibitory and substrate forms, and of their respective reactive-center cleaved forms
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Fa M., Bergstrom F., Karolin J., Johansson L.B., Ny T. Conformational studies of plasminogen activator inhibitor type 1 by fluorescence spectroscopy. Analysis of the reactive center of inhibitory and substrate forms, and of their respective reactive-center cleaved forms. Eur J Biochem. 267:2000;3729-3734. Nice illustration of the use of donor-donor energy migration to study protein conformation by FRET.
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Eur J Biochem
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Baneyx G., Baugh L., Vogel V. Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer. Proc Natl Acad Sci USA. 98:2001;14464-14468.
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Protein compactness measured by fluorescence energy transfer. Human carbonic anhydrase II is considerably expanded by the interaction of GroEL
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EMBO Rep
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Chakrabarty T., Xiao M., Cooke R., Selvin P.R. Holding two heads together: stability of the myosin II rod measured by resonance energy transfer between the heads. Proc Natl Acad Sci USA. 99:2002;6011-6016. LRET and FRET have been used to probe the stability of the coiled-coil rod of myosin. Of particular interest is the use of a comparison between LRET and FRET data to draw conclusions about the flexibility of the regulatory light chain of myosin.
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Proc Natl Acad Sci USA
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Chakrabarty, T.1
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