| pubmed-article:11607456 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11607456 | lifeskim:mentions | umls-concept:C0175627 | lld:lifeskim |
| pubmed-article:11607456 | lifeskim:mentions | umls-concept:C0036576 | lld:lifeskim |
| pubmed-article:11607456 | lifeskim:mentions | umls-concept:C1823381 | lld:lifeskim |
| pubmed-article:11607456 | lifeskim:mentions | umls-concept:C1883073 | lld:lifeskim |
| pubmed-article:11607456 | lifeskim:mentions | umls-concept:C0544726 | lld:lifeskim |
| pubmed-article:11607456 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11607456 | pubmed:dateCreated | 2001-10-18 | lld:pubmed |
| pubmed-article:11607456 | pubmed:abstractText | We investigated spectral holes burnt at 1.5 K into the origins of several tautomeric forms of mesoporphyrin IX-substituted horseradish peroxidase at pH 8 under pressures up to 2 MPa. From the pressure-induced lineshift the compressibility of the apoprotein could be determined. We found that the compressibility changed significantly when measured at different tautomer origins. It was concluded that there must be a correlation between the tautomer configurations of the chromophore and the actual structures of the apoprotein. As a consequence, specific conformational substates of the protein can be selected by optical selection of the associated tautomers. | lld:pubmed |
| pubmed-article:11607456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11607456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11607456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11607456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11607456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11607456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11607456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11607456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11607456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11607456 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11607456 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11607456 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11607456 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
| pubmed-article:11607456 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11607456 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:11607456 | pubmed:author | pubmed-author:FriedrichJJ | lld:pubmed |
| pubmed-article:11607456 | pubmed:author | pubmed-author:ZollfrankJJ | lld:pubmed |
| pubmed-article:11607456 | pubmed:author | pubmed-author:FidyJJ | lld:pubmed |
| pubmed-article:11607456 | pubmed:author | pubmed-author:VanderkooiJJ | lld:pubmed |
| pubmed-article:11607456 | pubmed:author | pubmed-author:GafertJJ | lld:pubmed |
| pubmed-article:11607456 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11607456 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11607456 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:11607456 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11607456 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11607456 | pubmed:pagination | 1029-33 | lld:pubmed |
| pubmed-article:11607456 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
| pubmed-article:11607456 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:11607456 | pubmed:articleTitle | Spectral hole burning and selection of conformational substates in chromoproteins. | lld:pubmed |
| pubmed-article:11607456 | pubmed:affiliation | Physikalisches Institut und Bayreuther Institut für Makromolekülforschung, Bayreuth, Germany. | lld:pubmed |
| pubmed-article:11607456 | pubmed:publicationType | Journal Article | lld:pubmed |
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