| pubmed-article:3298253 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3298253 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:3298253 | lifeskim:mentions | umls-concept:C0004654 | lld:lifeskim |
| pubmed-article:3298253 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:3298253 | lifeskim:mentions | umls-concept:C0184511 | lld:lifeskim |
| pubmed-article:3298253 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:3298253 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:3298253 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:3298253 | lifeskim:mentions | umls-concept:C0052898 | lld:lifeskim |
| pubmed-article:3298253 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:3298253 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:3298253 | pubmed:dateCreated | 1987-8-14 | lld:pubmed |
| pubmed-article:3298253 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3298253 | pubmed:abstractText | The aims of this work have been to express bacterio-opsin with minimal variation from the native primary structure and to improve the level of expression in Escherichia coli. We describe the construction of plasmids in which the bacterio-opsin gene contains only an additional methionine residue at the N terminus and in which the C-terminal aspartic acid encoded in the gene has been deleted to conform to the mature protein. In attempts to improve bacterio-opsin expression, a variety of expression plasmids were constructed in which the promoters and the ribosome-binding sequences were varied. Invariably, in these plasmids, translation but not transcription of the bacterio-opsin gene was limiting. A striking increase in expression of the gene occurred when the codons for several of the N-terminal amino acids were changed to increase the A = T content. Bacterio-opsin expressed in E. coli was degraded with a half-life of 8-10 min. The addition of hydrophobic signal sequences at the N terminus increased the half-life and overall yield of the protein. Bacterio-opsin thus produced regenerated the native bacteriorhodopsin-like chromophore and carried out light-dependent proton translocation at a rate comparable to that of the native bacterio-opsin prepared from the purple membrane. | lld:pubmed |
| pubmed-article:3298253 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3298253 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3298253 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3298253 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3298253 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3298253 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3298253 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3298253 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3298253 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:3298253 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3298253 | pubmed:author | pubmed-author:DoiTT | lld:pubmed |
| pubmed-article:3298253 | pubmed:author | pubmed-author:KhoranaH GHG | lld:pubmed |
| pubmed-article:3298253 | pubmed:author | pubmed-author:JayEE | lld:pubmed |
| pubmed-article:3298253 | pubmed:author | pubmed-author:SgaramellaVV | lld:pubmed |
| pubmed-article:3298253 | pubmed:author | pubmed-author:NassalMM | lld:pubmed |
| pubmed-article:3298253 | pubmed:author | pubmed-author:KarnikS SSS | lld:pubmed |
| pubmed-article:3298253 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3298253 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:3298253 | pubmed:volume | 262 | lld:pubmed |
| pubmed-article:3298253 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3298253 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3298253 | pubmed:pagination | 9255-63 | lld:pubmed |
| pubmed-article:3298253 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3298253 | pubmed:meshHeading | pubmed-meshheading:3298253-... | lld:pubmed |
| pubmed-article:3298253 | pubmed:meshHeading | pubmed-meshheading:3298253-... | lld:pubmed |
| pubmed-article:3298253 | pubmed:meshHeading | pubmed-meshheading:3298253-... | lld:pubmed |
| pubmed-article:3298253 | pubmed:meshHeading | pubmed-meshheading:3298253-... | lld:pubmed |
| pubmed-article:3298253 | pubmed:meshHeading | pubmed-meshheading:3298253-... | lld:pubmed |
| pubmed-article:3298253 | pubmed:meshHeading | pubmed-meshheading:3298253-... | lld:pubmed |
| pubmed-article:3298253 | pubmed:meshHeading | pubmed-meshheading:3298253-... | lld:pubmed |
| pubmed-article:3298253 | pubmed:meshHeading | pubmed-meshheading:3298253-... | lld:pubmed |
| pubmed-article:3298253 | pubmed:meshHeading | pubmed-meshheading:3298253-... | lld:pubmed |
| pubmed-article:3298253 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3298253 | pubmed:articleTitle | Structure-function studies on bacteriorhodopsin. II. Improved expression of the bacterio-opsin gene in Escherichia coli. | lld:pubmed |
| pubmed-article:3298253 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3298253 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3298253 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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