| pubmed-article:12381848 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12381848 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:12381848 | lifeskim:mentions | umls-concept:C0600364 | lld:lifeskim |
| pubmed-article:12381848 | lifeskim:mentions | umls-concept:C1527177 | lld:lifeskim |
| pubmed-article:12381848 | lifeskim:mentions | umls-concept:C0441513 | lld:lifeskim |
| pubmed-article:12381848 | lifeskim:mentions | umls-concept:C0303920 | lld:lifeskim |
| pubmed-article:12381848 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:12381848 | pubmed:dateCreated | 2002-10-16 | lld:pubmed |
| pubmed-article:12381848 | pubmed:abstractText | Bacterial periplasmic binding proteins (bPBPs) are specific for a wide variety of small molecule ligands. bPBPs undergo a large, ligand-mediated conformational change that can be linked to reporter functions to monitor ligand concentrations. This mechanism provides the basis of a general system for engineering families of reagentless biosensors that share a common physical signal transduction functionality and detect many different analytes. We demonstrate the facility of designing optical biosensors based on fluorophore conjugates using 8 environmentally sensitive fluorophores and 11 bPBPs specific for diverse ligands, including sugars, amino acids, anions, cations, and dipeptides. Construction of reagentless fluorescent biosensors relies on identification of sites that undergo a local conformational change in concert with the global, ligand-mediated hinge-bending motion. Construction of cysteine mutations at these locations then permits site-specific coupling of environmentally sensitive fluorophores that report ligand binding as changes in fluorescence intensity. For 10 of the bPBPs presented in this study, the three-dimensional receptor structure was used to predict the location of reporter sites. In one case, a bPBP sensor specific for glutamic and aspartic acid was designed starting from genome sequence information and illustrates the potential for discovering novel binding functions in the microbial genosphere using bioinformatics. | lld:pubmed |
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| pubmed-article:12381848 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12381848 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12381848 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12381848 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12381848 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12381848 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:12381848 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:12381848 | pubmed:author | pubmed-author:HellingaHomme... | lld:pubmed |
| pubmed-article:12381848 | pubmed:author | pubmed-author:de... | lld:pubmed |
| pubmed-article:12381848 | pubmed:author | pubmed-author:SmithJ JeffJJ | lld:pubmed |
| pubmed-article:12381848 | pubmed:author | pubmed-author:DwyerMary AMA | lld:pubmed |
| pubmed-article:12381848 | pubmed:author | pubmed-author:LoogerLoren... | lld:pubmed |
| pubmed-article:12381848 | pubmed:author | pubmed-author:SaliKevin MKM | lld:pubmed |
| pubmed-article:12381848 | pubmed:author | pubmed-author:PaavolaChad... | lld:pubmed |
| pubmed-article:12381848 | pubmed:author | pubmed-author:RizkShahir... | lld:pubmed |
| pubmed-article:12381848 | pubmed:author | pubmed-author:SadigovShamil... | lld:pubmed |
| pubmed-article:12381848 | pubmed:author | pubmed-author:ConradDavid... | lld:pubmed |
| pubmed-article:12381848 | pubmed:author | pubmed-author:LoewLeslieL | lld:pubmed |
| pubmed-article:12381848 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12381848 | pubmed:volume | 11 | lld:pubmed |
