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10.1016/j.virol.2015.01.015 http://scihub22266oqcxt.onion/10.1016/j.virol.2015.01.015 C4424107!4424107!25728298     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Virology 2015 ; ä (ä): 650-6 Nephropedia Template TP {{tp|p=25728298|t=2015. Old, New, and Widely True: the Bacteriophage T4 DNA Packaging Mechanism |pdf=|usr=}}{{25728298}} gab.com Text Old, New, and Widely True: the Bacteriophage T4 DNA Packaging Mechanism JO: Virology http://www.kidney.de/pget.php?&tw=1&pmid=25728298 #FOAvip DNA packaging into empty viral procapsids by ATP-driven motor proteins applies widely among viruses. Recent fluorescence studies of phage T4 reveal: 1) the small terminase subunit (TerS) synapses pac homologs by a two ring mechanism to gauge DNA maturation and allow packaging by the large terminase subunit (TerL); 2) translocation of linear DNA is efficient by TerL acting alone; expansion of the procapsid is controlled by the portal-terminase assembly; 3) both ends of the packaged DNA are held at the portal, showing a loop of DNA is packaged; 4) transient spring-like compression of B form to A form-like DNA accompanies translocation; 5) the C-terminal domain of TerL is docked to the portal and moves toward it when stalled; 6) a portal bound resolvase can release stalled Y-DNA compression and allow translocation in vitro; and 7) ATP powered translocation on A form dsDNA is supported by recent hexameric helicase studies. Twit Text FOAVip Old, New, and Widely True: the Bacteriophage T4 DNA Packaging Mechanism ????Virology http://www.kidney.de/pget.php?&tw=1&pmid=25728298 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25728298 #FOAvip English Wikipedia <ref>{{Cite pmid|25728298}}</ref> Old, New, and Widely True: the Bacteriophage T4 DNA Packaging Mechanism #MMPMID25728298 Black LW Virology 2015[May]; ä (ä): 650-6 PMID25728298show ga DNA packaging into empty viral procapsids by ATP-driven motor proteins applies widely among viruses. Recent fluorescence studies of phage T4 reveal: 1) the small terminase subunit (TerS) synapses pac homologs by a two ring mechanism to gauge DNA maturation and allow packaging by the large terminase subunit (TerL); 2) translocation of linear DNA is efficient by TerL acting alone; expansion of the procapsid is controlled by the portal-terminase assembly; 3) both ends of the packaged DNA are held at the portal, showing a loop of DNA is packaged; 4) transient spring-like compression of B form to A form-like DNA accompanies translocation; 5) the C-terminal domain of TerL is docked to the portal and moves toward it when stalled; 6) a portal bound resolvase can release stalled Y-DNA compression and allow translocation in vitro; and 7) ATP powered translocation on A form dsDNA is supported by recent hexameric helicase studies. äOld, New, and Widely True: the Bacteriophage T4 DNA Packaging Mechanis(epmc).pdf DeepDyve Pubget Overpricing