31 research outputs found
Identification of an expanded set of translationally active methionine analogues in Escherichia coli
Amino acid incorporation into proteins in vivo is controlled most stringently by the aminoacyl-tRNA synthetases. Here we report the incorporation of several new methionine analogues into protein by increasing the rate of their activation by the methionyl-tRNA synthetase (MetRS) of Escherichia coli. cis-Crotylglycine (4), 2-aminoheptanoic acid (7), norvaline (8), 2-butynylglycine (11), and allylglycine (12) will each support protein synthesis in methionine-depleted cultures of E. coli when MetRS is overexpressed and the medium is supplemented with the analogue at millimolar concentrations. These investigations suggest important opportunities for protein engineering, as expansion of the translational apparatus toward other amino acid analogues by similar strategies should also be possible
Fine-tuning the transition temperature of a stimuli-responsive polymer by a simple blending procedure
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Reversible Immobilization onto PEG-based Emulsion-templated Porous Polymers by Co-assembly of Stimuli Responsive Polymers
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Covalent enzyme immobilization onto photopolymerized highly porous monoliths
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