| pubmed-article:14971914 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14971914 | lifeskim:mentions | umls-concept:C0027078 | lld:lifeskim |
| pubmed-article:14971914 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:14971914 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:14971914 | lifeskim:mentions | umls-concept:C1880371 | lld:lifeskim |
| pubmed-article:14971914 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:14971914 | pubmed:dateCreated | 2004-2-19 | lld:pubmed |
| pubmed-article:14971914 | pubmed:abstractText | We used femtosecond infrared polarization spectroscopy and density functional theory in a study on the key signaling molecule nitric oxide (NO) bound to myoglobin. Our results show that after photolysis, a substantial fraction of NO recombines within the first few picoseconds. We discovered that the diatomic ligand is severely tilted in the protein and present evidence that the Fe-NO moiety can sample a wide range of off-axis tilting and bending conformations. | lld:pubmed |
| pubmed-article:14971914 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14971914 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14971914 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14971914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14971914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14971914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14971914 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14971914 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:14971914 | pubmed:issn | 0002-7863 | lld:pubmed |
| pubmed-article:14971914 | pubmed:author | pubmed-author:HeyneKarstenK | lld:pubmed |
| pubmed-article:14971914 | pubmed:author | pubmed-author:DandekarThoma... | lld:pubmed |
| pubmed-article:14971914 | pubmed:author | pubmed-author:RiniMatteoM | lld:pubmed |
| pubmed-article:14971914 | pubmed:author | pubmed-author:NibberingErik... | lld:pubmed |
| pubmed-article:14971914 | pubmed:author | pubmed-author:KozlowskiPawe... | lld:pubmed |
| pubmed-article:14971914 | pubmed:author | pubmed-author:ZemojtelTomas... | lld:pubmed |
| pubmed-article:14971914 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14971914 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:14971914 | pubmed:volume | 126 | lld:pubmed |
| pubmed-article:14971914 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14971914 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14971914 | pubmed:pagination | 1930-1 | lld:pubmed |
| pubmed-article:14971914 | pubmed:dateRevised | 2008-1-17 | lld:pubmed |
| pubmed-article:14971914 | pubmed:meshHeading | pubmed-meshheading:14971914... | lld:pubmed |
| pubmed-article:14971914 | pubmed:meshHeading | pubmed-meshheading:14971914... | lld:pubmed |
| pubmed-article:14971914 | pubmed:meshHeading | pubmed-meshheading:14971914... | lld:pubmed |
| pubmed-article:14971914 | pubmed:meshHeading | pubmed-meshheading:14971914... | lld:pubmed |
| pubmed-article:14971914 | pubmed:meshHeading | pubmed-meshheading:14971914... | lld:pubmed |
| pubmed-article:14971914 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14971914 | pubmed:articleTitle | NO-bound myoglobin: structural diversity and dynamics of the NO ligand. | lld:pubmed |
| pubmed-article:14971914 | pubmed:affiliation | Department of Bioinformatics, University of Wuerzburg, Am Hubland, D-97074 Wuerzburg, Germany. zemojtel@biozentrum.uni-wuerzburg.de | lld:pubmed |
| pubmed-article:14971914 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14971914 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14971914 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14971914 | lld:pubmed |
