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10.1073/pnas.1503533112 http://scihub22266oqcxt.onion/10.1073/pnas.1503533112 C4403210!4403210!25831510     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       Proc+Natl+Acad+Sci+U+S+A 2015 ; 112 (15): 4564-9 Nephropedia Template TP {{tp|p=25831510|t=2015. DNA-mediated engineering of multicomponent enzyme crystals |pdf=|usr=}}{{25831510}} gab.com Text DNA-mediated engineering of multicomponent enzyme crystals JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25831510 #FOAvip Due to their unique structures and diverse catalytic functionalities, proteins represent a nearly limitless set of precursors for constructing functional supramolecular materials. However, programming the assembly of even a single protein into ordered superlattices is a difficult task, and a generalizable strategy for coassembling multiple proteins with distinct surface chemistries, or proteins and inorganic nanoparticles, does not currently exist. Here, we use the high-fidelity interactions characteristic of DNA?DNA ?bonds? to direct the assembly of two proteins into six unique superlattices composed of either a single protein, multiple proteins, or proteins and gold nanoparticles. Significantly, the DNA-functionalized proteins retain their native catalytic functionalities both in the solution and crystalline states. Twit Text FOAVip DNA-mediated engineering of multicomponent enzyme crystals ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25831510 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25831510 #FOAvip English Wikipedia <ref>{{Cite pmid|25831510}}</ref> DNA-mediated engineering of multicomponent enzyme crystals #MMPMID25831510 Brodin JD; Auyeung E; Mirkin CA Proc Natl Acad Sci U S A 2015[Apr]; 112 (15): 4564-9 PMID25831510show ga Due to their unique structures and diverse catalytic functionalities, proteins represent a nearly limitless set of precursors for constructing functional supramolecular materials. However, programming the assembly of even a single protein into ordered superlattices is a difficult task, and a generalizable strategy for coassembling multiple proteins with distinct surface chemistries, or proteins and inorganic nanoparticles, does not currently exist. Here, we use the high-fidelity interactions characteristic of DNA?DNA ?bonds? to direct the assembly of two proteins into six unique superlattices composed of either a single protein, multiple proteins, or proteins and gold nanoparticles. Significantly, the DNA-functionalized proteins retain their native catalytic functionalities both in the solution and crystalline states. äDNA-mediated engineering of multicomponent enzyme crystals (epmc).pdf DeepDyve Pubget Overpricing