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10.1016/j.tig.2014.09.004 http://scihub22266oqcxt.onion/10.1016/j.tig.2014.09.004 C4254034!4254034!25306102     free     free     free       Trends+Genet 2014 ; 30 (12): 521-8 Nephropedia Template TP {{tp|p=25306102|t=2014. Engineering Allostery |pdf=|usr=}}{{25306102}} gab.com Text Engineering Allostery JO: Trends Genet http://www.kidney.de/pget.php?&tw=1&pmid=25306102 #FOAvip Allosteric proteins have great potential in synthetic biology, but our limited understanding of the molecular underpinnings of allostery has hindered the development of designer molecules, including transcription factors with new DNA-binding or ligand-binding specificities that respond appropriately to inducers. Such allosteric proteins could function as novel switches in complex circuits, metabolite sensors, or orthogonal regulators for independent, inducible control of multiple genes. Advances in DNA synthesis and next-generation sequencing technologies have enabled the assessment of millions of mutants in a single experiment, providing new opportunities to study allostery. Using the classic LacI protein as an example, we describe a genetic selection system using a bidirectional reporter to capture mutants in both allosteric states, allowing the positions most critical for allostery to be identified. This approach is not limited to bacterial transcription factors, and could reveal new mechanistic insights and facilitate engineering of other major classes of allosteric proteins such as nuclear receptors, two-component systems, G-protein coupled receptors and protein kinases. Twit Text FOAVip Engineering Allostery ????Trends Genet http://www.kidney.de/pget.php?&tw=1&pmid=25306102 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25306102 #FOAvip English Wikipedia <ref>{{Cite pmid|25306102}}</ref> Engineering Allostery #MMPMID25306102 Raman S; Taylor N; Genuth N; Fields S; Church GM Trends Genet 2014[Dec]; 30 (12): 521-8 PMID25306102show ga Allosteric proteins have great potential in synthetic biology, but our limited understanding of the molecular underpinnings of allostery has hindered the development of designer molecules, including transcription factors with new DNA-binding or ligand-binding specificities that respond appropriately to inducers. Such allosteric proteins could function as novel switches in complex circuits, metabolite sensors, or orthogonal regulators for independent, inducible control of multiple genes. Advances in DNA synthesis and next-generation sequencing technologies have enabled the assessment of millions of mutants in a single experiment, providing new opportunities to study allostery. Using the classic LacI protein as an example, we describe a genetic selection system using a bidirectional reporter to capture mutants in both allosteric states, allowing the positions most critical for allostery to be identified. This approach is not limited to bacterial transcription factors, and could reveal new mechanistic insights and facilitate engineering of other major classes of allosteric proteins such as nuclear receptors, two-component systems, G-protein coupled receptors and protein kinases. äEngineering Allostery (epmc).pdf DeepDyve Pubget Overpricing