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Gryczynski, Z.1
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Nomambhoy, T.K.1
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Keller, R.C.A.1
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Evidence for coupling of folding and function in trp repressor: Physical characterization of the super-repressor mutant AV77
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Characterization of charge-change super-repressor mutants of trp repressor: Effects on oligomerization, conformation, ligation, and stability
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21. Reedstrom RJ, Martin KS, Vangala S, Mahoney S, Wilker EW, Royer CA: Characterization of charge-change super-repressor mutants of trp repressor: effects on oligomerization, conformation, ligation, and stability. J Mol Biol 1996, in press.
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Electrostatic forces contribute to interactions between trp repressor dimers
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Martin, K.S.1
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Berland, K.M.1
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Anti-cooperative biphasic equilibrium binding of transcription factor upstream stimulatory factor to its cognate DNA monitored by protein fluorescence changes
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Sha, M.1
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Individual subunits of heterodimers comprised of retinoic acid and retinoid X receptors interact with their ligands independently
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26. Kersten S, Dawson MI, Lewis BA, Noy N: Individual subunits of heterodimers comprised of retinoic acid and retinoid X receptors interact with their ligands independently. Biochemistry 1996, 35:3816-3824.
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27. Carver TE, Hochstrasser RA, Millar DP: Proofreading DNA: recognition of aberrant DNA termini by the Klenow fragment of DNA polymerase I. Proc Natl Acad Sci USA 1994, 91:10670-10674.
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Interaction of DNA with the Klenow fragment of DNA polymerase I studied by time-resolved fluorescence spectroscopy
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Guest, C.R.1
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Interaction between the Escherichia coli regulatory protein TyrR and DNA: A fluorescence footprinting study
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29. Bailey M, Hagmar P, Millar DP, Davidson BE, Tong G, Haralambidis J, Sawyer WH: Interaction between the Escherichia coli regulatory protein TyrR and DNA: a fluorescence footprinting study. Biochemistry 1995, 34:15802-15812. This paper is an excellent example of the fluorescence footprinting technique, and it builds upon the seminal work of Guest et al. [28] and Carver et al. [27].
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Biochemistry
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Bailey, M.1
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32. Hill JJ, Royer CA: Fluorescence approaches to the study of protein-nucleic acid complexation. Methods Enzymol 1996, in press. This is an excellent review for those interested in using fluorescence to study protein-DNA interactions, and it provides useful, practical advice.
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Methods Enzymol
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Hill, J.J.1
Royer, C.A.2
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Yeast TATA binding protein interaction with DNA: Fluorescence determination of oligomeric state, equilibrium binding, on-rate, and dissociation kinetics
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33. Perez-Howard GM, Weil PA, Beechem JM: Yeast TATA binding protein interaction with DNA: fluorescence determination of oligomeric state, equilibrium binding, on-rate, and dissociation kinetics. Biochemistry 1995, 34:8005-8017. With rhodamine-X covalently bound to the 5′-end of an oligonucleotide, these authors examine the kinetics of a protein-DNA interaction using stopped-flow instrumentation measuring the anisotropy of rhodamine X. This is the first reported study of its kind, and presents a new and useful technique for the study of protein-DNA binding.
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Perez-Howard, G.M.1
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Hybridization of fluorescein-labeled DNA oligomers detected by fluorescence anisotropy with protein binding enhancement
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34. Kumke MU, Li G, McGowan LA, Walker GT, Linn CP: Hybridization of fluorescein-labeled DNA oligomers detected by fluorescence anisotropy with protein binding enhancement. Anal Chem 1995, 67:3945-3951. This paper presents a new method for monitoring DNA hybridization by adding a double-stranded protein binding site to the oligonucleotide being examined in order to sufficiently increase the change in anisotropy of a 5′-end bound fluorophore upon DNA hybridization. In addition, this is an excellent study of the effect of tether length and protein binding site location on protein-induced fluorescence signal changes of the 5′-end bound fluorophore. The authors find that a six-carbon tether and a protein-binding site as close as possible to the 5′-end provide the largest change in anisotropy for both DNA-DNA and DNA-protein interactions when fluorescein is the fluorophore.
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Kumke, M.U.1
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35. Vamosi G, Gohlke C, Clegg RM: Fluorescence characteristics of 5-carboxytetramethylrhodamine linked covalently to the 5′ end of oligonucleotides: multiple conformers of single-stranded and double-stranded dye-DNA complexes. Biophys J 1996, 71:972-994. This is an excellent, in-depth study of the fluorescence characteristics of the THRh-DNA complex. The authors find that there are three TMRh-DNA species, two that are light and one that is dark, the relative distribution of which is shown to be modulated by salt concentration. The authors emphasize that until rigorous physical and spectroscopic studies are performed with other dye-DNA complexes, the interpretation of any data collected using such a complex is severely limited.
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Biophys J
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Vamosi, G.1
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