Part:BBa_K1790000:Design
biosensors detect food allergens. A proteins conformation change in response to ligand binding coupl
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 990
Illegal BglII site found at 1068
Illegal XhoI site found at 67 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 316
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI.rc site found at 1017
GLN_H gene source
E.Coli - E. coli bacteria were discovered in the human colon in 1885 by German bacteriologist Theodor Escherich. E. coli is often referred to as the best or most-studied free-living organism. More than 700 serotypes of E. coli have been identified. The E. coli that are responsible for the numerous reports of contaminated foods and beverages are those that produce Shiga toxin, so called because the toxin is virtually identical to that produced by Shigella dysenteria type 1 The bacterium can be grown and cultured easily and inexpensively in a laboratory setting, and has been intensively investigated for over 60 years. E. coli is the most widely studied prokaryotic model organism, and an important species in the fields of biotechnology and microbiology, where it has served as the host organism for the majority of work with recombinant DNA E. coli is a Gram-negative (bacteria which do not retain crystal violet dye), facultative anaerobic (that makes ATP by aerobic respiration if oxygen is present, but is capable of switching to fermentation or anaerobic respiration if oxygen is absent) and nonsporulating bacteria.
Our biosensor
Our protein
The Gln-H protein after adding the linkers. The linkers added to the ends of the C terminal and N terminal. This mutation cycle allows one of the new Terminal ends of the protein to unite (when on each end is half of another reporter gene), in actual fact the two parts of the gene come together and form comfortable conditions for creating color. The change in color will occur only when the connection is through gluten. The mutation protein will act as follows: Without gluten - the protein will be in the open position and therefore the half enzyme will remain inactive and there will not be a color reaction. The presence of gluten - the protein closes, following; the half enzyme will close and become an active enzyme with the result of a color reaction.
References
Daniel Leffler, MD, MS, The Celiac Center at Beth Israel Deaconness Medical Center Datamonitor Group, 2009, Packaged Facts, 2011 ahttp://www.biocyc.org/ECOLI/NEW-IMAGE?type=GENE&object=G6932
Satoshi Okada et al. (2009) Circular permutation of ligand-binding module improves dynamic range of genetically encoded FRET-based nanosensor. Department of Computational Biology, Graduate School of Frontier Sciences, University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa 277-8561, Japan
Katrin Gruenwald1 et al. (2012) Visualization of Glutamine Transporter Activities in Living Cells Using Genetically Encoded Glutamine Sensors. Department of Plant Pathology, Physiology and Weed Science, Virginia Tech, Blacksburg, Virginia, United States of America, 2 Department of Botany, Faculty of Science, Hamdard University, New Delhi, India
Fabio Cimaglia et al. (2014) Study of a New Gliadin Capture Agent and Development of a Protein Microarray as a New Approach for Gliadin Detection Biotecgen srl, Lecce, Italy 2 Consiglio Nazionale delle Ricerche- Istituto di Scienze delle Produzioni Alimentari, Unità Operativa di Lecce, Lecce, Italy
Ste´phanie Cabantous et al (2013). A New Protein-Protein Interaction Sensor Based on Tripartite Split-GFP Association. INSERM UMR1037, Cancer Research Center of Toulouse, Universite´ de Toulouse, Institut Claudius Regaud, F-31052 Toulouse, France, 2 Bioscience Division, MS-M888, Los Alamos National Laboratory, Los Alamos, NM 87545, USA, 3 CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), F-31077 Toulouse, France; Universite´ de Toulouse; UPS, IPBS, F-31077 Toulouse, France, 4 Department of Microbiology, University of Washington, Seattle, WA 98195, USA, 5 Rockefeller University, New York, NY 10065, USA
Alessio Ausili et al (2013). Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga maritima: A Brief Thermo-Story. Laboratory for Molecular Sensing, Institute of Protein Biochemistry, CNR, Via Pietro Castellino, 111, Napoli, 80131, Italy; E-Mails: a.ausili@ibp.cnr.it (A.A.); m.staiano@ibp.cnr.it (M.S.); a.varriale@ibp.cnr.it (A.V.); a.capo@ibp.cnr.it (A.C.) 2 Department of Chemistry, University of Richmond, Richmond, VA 23173, USA; E-Mail: jdattelb@richmond.edu