Dark Matter eLiquid

Enjoy the wonderful flavor of our latest VapeSafe eLiquid - Dark Matter.

Dark Matter tastes like German chocolate cake. For those of you who have not had the fortunate to try a piece German chocolate cake recently, this is a great way to experience the flavor without getting any of the calories. German chocolate cake is a layered cake filled and topped with a coconut-pecan frosting. Traditionally sweet baking chocolate is used for the chocolate flavor in the actual cake. The robust filling and topping is a caramel made with egg yolks and evaporated milk. Once the caramel is cooked, coconut and pecans are stirred into the mixture. Finally, rich chocolate frosting is spread around the sides of the cake to hold in the filling.

Dark Matter eLiquid by VapeSafe captures the essence of German chocolate cake. Dark Matter eLiquid delivers plumes of vapor and rich chocolatey flavor that you'll want to enjoy again and again. Try Dark Matter today!

Technology Information:

lQ interaction with E. coli RNA polymerase for antitermination: Regions of E. coli RNA polymerase required for lQ-mediated antitermination in binding and function

Description

Phage lQ protein is a transcriptional antiterminator that is required for late gene expression from the pR prime promoter when lambda prophage decides to follow the lytic pathway. lQ modifies Escherichia coli RNA polymerase (RNAP) at the early elongation stage. Once engaged, lQ maintains itself as a subunit of the elongation complex throughout the elongation. Studies show that lQ confers RNAP resistance to both intrinsic and rho-mediated terminators and less pausing. However, little is known about the interaction between lQ and RNAP. In this study, the largest subunits (beta and beta prime) of RNAP were examined to map the lQ binding site. A stronger binding was observed with beta than beta prime, and the binding site was narrowed to beta 501-832. This region was further defined as small as 82 amino acids (beta 600-681) that interacted with lQ. In addition, 12 mutant RNAPs were isolated for a reduced lQ antitermination within the potential lQ binding regions, specifically near the main channel. These results propose that lQ modifies the active center of RNAP for antitermination.

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