906734-92-7Relevant articles and documents
Light Regulation of Enzyme Allostery through Photo-responsive Unnatural Amino Acids
Kneuttinger, Andrea C.,Straub, Kristina,Bittner, Philipp,Simeth, Nadja A.,Bruckmann, Astrid,Busch, Florian,Rajendran, Chitra,Hupfeld, Enrico,Wysocki, Vicki H.,Horinek, Dominik,K?nig, Burkhard,Merkl, Rainer,Sterner, Reinhard
, p. 1501 - 9,1514 (2019)
Imidazole glycerol phosphate synthase (ImGPS) is an allosteric bienzyme complex in which substrate binding to the synthase subunit HisF stimulates the glutaminase subunit HisH. To control this stimulation with light, we have incorporated the photo-respons
Modulating the Phe-Phe dipeptide aggregation landscape via covalent attachment of an azobenzene photoswitch
Johny, Melby,Vijayalakshmi, Kanchustambham,Das, Ankita,Roy, Palas,Mishra, Aseem,Dasgupta, Jyotishman
, p. 9348 - 9351 (2017)
Synthetic control of peptide-based supramolecular assemblies can provide molecular cues to understand protein aggregation while also inspiring the development of novel chemical biology tools to deliver cargoes inside cells. Here we show that the trans-to-
The incorporation of a photoisomerizable amino acid into proteins in E. coli
Bose, Mohua,Groff, Dan,Xie, Jianming,Brustad, Eric,Schultz, Peter G.
, p. 388 - 389 (2007/10/03)
An orthogonal aminoacyl tRNA synthetase/tRNA pair has been evolved that allows the incorporation of the photoisomerizable amino acid phenylalanine-4′-azobenzene (AzoPhe) into proteins in E. coli in response to the amber nonsense codon. Further, we show th
