pubmed-article:8650577 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8650577 | lifeskim:mentions | umls-concept:C0007271 | lld:lifeskim |
pubmed-article:8650577 | lifeskim:mentions | umls-concept:C0023693 | lld:lifeskim |
pubmed-article:8650577 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:8650577 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
pubmed-article:8650577 | lifeskim:mentions | umls-concept:C0996357 | lld:lifeskim |
pubmed-article:8650577 | pubmed:issue | 5269 | lld:pubmed |
pubmed-article:8650577 | pubmed:dateCreated | 1996-7-25 | lld:pubmed |
pubmed-article:8650577 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8650577 | pubmed:abstractText | Peridinin-chlorophyll-protein, a water-soluble light-harvesting complex that has a blue-green absorbing carotenoid as its main pigment, is present in most photosynthetic dinoflagellates. Its high-resolution (2.0 angstrom) x-ray structure reveals a noncrystallographic trimer in which each polypeptide contains an unusual jellyroll fold of the alpha-helical amino- and carboxyl-terminal domains. These domains constitute a scaffold with pseudo-twofold symmetry surrounding a hydrophobic cavity filled by two lipid, eight peridinin, and two chlorophyll a molecules. The structural basis for efficient excitonic energy transfer from peridinin to chlorophyll is found in the clustering of peridinins around the chlorophylls at van der Waals distances. | lld:pubmed |
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pubmed-article:8650577 | pubmed:language | eng | lld:pubmed |
pubmed-article:8650577 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8650577 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8650577 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8650577 | pubmed:month | Jun | lld:pubmed |
pubmed-article:8650577 | pubmed:issn | 0036-8075 | lld:pubmed |
pubmed-article:8650577 | pubmed:author | pubmed-author:HofmannEE | lld:pubmed |
pubmed-article:8650577 | pubmed:author | pubmed-author:HillerR GRG | lld:pubmed |
pubmed-article:8650577 | pubmed:author | pubmed-author:WrenchP MPM | lld:pubmed |
pubmed-article:8650577 | pubmed:author | pubmed-author:WelteWW | lld:pubmed |
pubmed-article:8650577 | pubmed:author | pubmed-author:DiederichsKK | lld:pubmed |
pubmed-article:8650577 | pubmed:author | pubmed-author:SharplesF PFP | lld:pubmed |
pubmed-article:8650577 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8650577 | pubmed:day | 21 | lld:pubmed |
pubmed-article:8650577 | pubmed:volume | 272 | lld:pubmed |
pubmed-article:8650577 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8650577 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8650577 | pubmed:pagination | 1788-91 | lld:pubmed |
pubmed-article:8650577 | pubmed:dateRevised | 2007-3-19 | lld:pubmed |
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pubmed-article:8650577 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8650577 | pubmed:articleTitle | Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae. | lld:pubmed |
pubmed-article:8650577 | pubmed:affiliation | Fakultät für Biologie, Universität Konstanz, Germany. | lld:pubmed |
pubmed-article:8650577 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8650577 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
family:PF02429.10 | family:pubmed | pubmed-article:8650577 | lld:pfam |
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