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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2001-10-18
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-13837237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-1504243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-1547326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-1749933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-19431865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-2166599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-3004569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-3293595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-3860839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-4041549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-460437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607456-6572366
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pubmed:language |
eng
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pubmed:journal |
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pubmed:status |
PubMed-not-MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1029-33
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pubmed:dateRevised |
2010-9-14
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pubmed:year |
1994
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pubmed:articleTitle |
Spectral hole burning and selection of conformational substates in chromoproteins.
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pubmed:affiliation |
Physikalisches Institut und Bayreuther Institut für Makromolekülforschung, Bayreuth, Germany.
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pubmed:publicationType |
Journal Article
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