| pubmed-article:9836635 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9836635 | pubmed:issue | 5395 | lld:pubmed |
| pubmed-article:9836635 | pubmed:dateCreated | 1998-12-28 | lld:pubmed |
| pubmed-article:9836635 | pubmed:abstractText | Enzymatic turnovers of single cholesterol oxidase molecules were observed in real time by monitoring the emission from the enzyme's fluorescent active site, flavin adenine dinucleotide (FAD). Statistical analyses of single-molecule trajectories revealed a significant and slow fluctuation in the rate of cholesterol oxidation by FAD. The static disorder and dynamic disorder of reaction rates, which are essentially indistinguishable in ensemble-averaged experiments, were determined separately by the real-time single-molecule approach. A molecular memory phenomenon, in which an enzymatic turnover was not independent of its previous turnovers because of a slow fluctuation of protein conformation, was evidenced by spontaneous spectral fluctuation of FAD. | lld:pubmed |
| pubmed-article:9836635 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9836635 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9836635 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9836635 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9836635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9836635 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9836635 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9836635 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:9836635 | pubmed:author | pubmed-author:TUY CYC | lld:pubmed |
| pubmed-article:9836635 | pubmed:author | pubmed-author:LIUT STS | lld:pubmed |
| pubmed-article:9836635 | pubmed:author | pubmed-author:LuH PHP | lld:pubmed |
| pubmed-article:9836635 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9836635 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:9836635 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:9836635 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9836635 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9836635 | pubmed:pagination | 1877-82 | lld:pubmed |
| pubmed-article:9836635 | pubmed:dateRevised | 2007-3-19 | lld:pubmed |
| pubmed-article:9836635 | pubmed:meshHeading | pubmed-meshheading:9836635-... | lld:pubmed |
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| pubmed-article:9836635 | pubmed:meshHeading | pubmed-meshheading:9836635-... | lld:pubmed |
| pubmed-article:9836635 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9836635 | pubmed:articleTitle | Single-molecule enzymatic dynamics. | lld:pubmed |
| pubmed-article:9836635 | pubmed:affiliation | Pacific Northwest National Laboratory, William R. Wiley Environmental Molecular Sciences Laboratory, Richland, WA 99352, USA. | lld:pubmed |
| pubmed-article:9836635 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9836635 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:9836635 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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