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10.1016/j.bpj.2014.07.024 http://scihub22266oqcxt.onion/10.1016/j.bpj.2014.07.024 C4156673!4156673 !25185556     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25185556 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biophys+J 2014 ; 107 (5 ): 1205-1216 Nephropedia Template TP {{tp|p=25185556 |t=2014. Tethered fluorophore motion: studying large DNA conformational changes by single-fluorophore imaging |pdf=|usr=}}{{25185556 }} gab.com Text Tethered fluorophore motion: studying large DNA conformational changes by single-fluorophore imaging JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25185556 #FOAvip We have previously introduced tethered fluorophore motion (TFM), a single-molecule fluorescence technique that monitors the effective length of a biopolymer such as DNA. TFM uses the same principles as tethered particle motion (TPM) but employs a single fluorophore in place of the bead, allowing TFM to be combined with existing fluorescence techniques on a standard fluorescence microscope. TFM has been previously been used to reveal the mechanism of two site-specific recombinase systems, Cre-loxP and XerCD-dif. In this work, we characterize TFM, focusing on the theoretical basis and potential applications of the technique. Since TFM is limited in observation time and photon count by photobleaching, we present a description of the sources of noise in TFM. Comparing this with Monte Carlo simulations and experimental data, we show that length changes of 100 bp of double-stranded DNA are readily distinguishable using TFM, making it comparable with TPM. We also show that the commonly recommended pixel size for single-molecule fluorescence approximately optimizes signal to noise for TFM experiments, thus enabling facile combination of TFM with other fluorescence techniques, such as Förster resonance energy transfer (FRET). Finally, we apply TFM to determine the polymerization rate of the Klenow fragment of DNA polymerase I, and we demonstrate its combination with FRET to observe synapsis formation by Cre using excitation by a single laser. We hope that TFM will be a useful addition to the single-molecule toolkit, providing excellent insight into protein-nucleic acid interactions. Twit Text FOAVip Tethered fluorophore motion: studying large DNA conformational changes by single-fluorophore imaging ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25185556 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25185556 #FOAvip English Wikipedia <ref>{{Cite pmid|25185556 }}</ref> Tethered fluorophore motion: studying large DNA conformational changes by single-fluorophore imaging #MMPMID25185556 May PFJ ; Pinkney JNM ; Zawadzki P ; Evans GW ; Sherratt DJ ; Kapanidis AN Biophys J 2014[Sep]; 107 (5 ): 1205-1216 PMID25185556 show ga We have previously introduced tethered fluorophore motion (TFM), a single-molecule fluorescence technique that monitors the effective length of a biopolymer such as DNA. TFM uses the same principles as tethered particle motion (TPM) but employs a single fluorophore in place of the bead, allowing TFM to be combined with existing fluorescence techniques on a standard fluorescence microscope. TFM has been previously been used to reveal the mechanism of two site-specific recombinase systems, Cre-loxP and XerCD-dif. In this work, we characterize TFM, focusing on the theoretical basis and potential applications of the technique. Since TFM is limited in observation time and photon count by photobleaching, we present a description of the sources of noise in TFM. Comparing this with Monte Carlo simulations and experimental data, we show that length changes of 100 bp of double-stranded DNA are readily distinguishable using TFM, making it comparable with TPM. We also show that the commonly recommended pixel size for single-molecule fluorescence approximately optimizes signal to noise for TFM experiments, thus enabling facile combination of TFM with other fluorescence techniques, such as Förster resonance energy transfer (FRET). Finally, we apply TFM to determine the polymerization rate of the Klenow fragment of DNA polymerase I, and we demonstrate its combination with FRET to observe synapsis formation by Cre using excitation by a single laser. We hope that TFM will be a useful addition to the single-molecule toolkit, providing excellent insight into protein-nucleic acid interactions. |*Nucleic Acid Conformation [MESH] |Computer Simulation [MESH] |DNA Polymerase I/chemistry [MESH] |DNA/*chemistry [MESH] |Diffusion [MESH] |Escherichia coli [MESH] |Fluorescent Dyes/*chemistry [MESH] |Microscopy, Fluorescence/*methods [MESH] |Models, Molecular [MESH] |Monte Carlo Method [MESH] |Motion [MESH] |Polymerization [MESH]Tethered fluorophore motion: studying large DNA conformational changes(epmc).pdf DeepDyve Pubget Overpricing