| pubmed-article:12944301 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12944301 | lifeskim:mentions | umls-concept:C0018893 | lld:lifeskim |
| pubmed-article:12944301 | lifeskim:mentions | umls-concept:C0006732 | lld:lifeskim |
| pubmed-article:12944301 | lifeskim:mentions | umls-concept:C0037098 | lld:lifeskim |
| pubmed-article:12944301 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:12944301 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:12944301 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:12944301 | lifeskim:mentions | umls-concept:C0016315 | lld:lifeskim |
| pubmed-article:12944301 | lifeskim:mentions | umls-concept:C2346927 | lld:lifeskim |
| pubmed-article:12944301 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:12944301 | lifeskim:mentions | umls-concept:C1060974 | lld:lifeskim |
| pubmed-article:12944301 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:12944301 | pubmed:dateCreated | 2003-8-28 | lld:pubmed |
| pubmed-article:12944301 | pubmed:abstractText | The calcium-binding protein isolated from the sarcoplasm of the muscles of the sand worm Nereis diversicolor has four EF-hands and three active binding sites for Ca(2+) or Mg(2+). Nereis diversicolor sarcoplasmic calcium-binding protein contains three tryptophan residues at positions 4, 57, and 170, respectively. The Wt protein shows a very limited fluorescence increase upon binding of Ca(2+) or Mg(2+). Single-tryptophan-containing mutants were produced and purified. The fluorescence titrations of these mutants show a limited decrease of the affinity for calcium, but no alterations of the cooperativity. Upon adding calcium, Trp170 shows a strong fluorescence increase, Trp57 an extensive fluorescence decrease, and Trp4 shows no fluorescence change. Therefore mutant W4F/W170F is ideally suited to analyze the fluorescence titrations and to study the binding mechanism. Mutations of the calcium ligands at the z-position in the three binding sites show no effect at site I and a total loss of cooperativity at sites III and IV. The quenching of Trp57 upon calcium binding is dependent on the presence of arginine R25, but this residue is not just a simple dynamic quencher. The role of the salt bridge R25-D58 is also investigated. | lld:pubmed |
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| pubmed-article:12944301 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12944301 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12944301 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12944301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12944301 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12944301 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:12944301 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:12944301 | pubmed:author | pubmed-author:RobbenJohanJ | lld:pubmed |
| pubmed-article:12944301 | pubmed:author | pubmed-author:VolckaertGuid... | lld:pubmed |
| pubmed-article:12944301 | pubmed:author | pubmed-author:VerheydenStef... | lld:pubmed |
| pubmed-article:12944301 | pubmed:author | pubmed-author:EngelborghsYv... | lld:pubmed |
| pubmed-article:12944301 | pubmed:author | pubmed-author:SillenAlainA | lld:pubmed |
| pubmed-article:12944301 | pubmed:author | pubmed-author:DelfosseLotte... | lld:pubmed |
| pubmed-article:12944301 | pubmed:author | pubmed-author:BraemTaniaT | lld:pubmed |
| pubmed-article:12944301 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12944301 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:12944301 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12944301 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12944301 | pubmed:pagination | 1882-93 | lld:pubmed |
| pubmed-article:12944301 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:12944301 | pubmed:meshHeading | pubmed-meshheading:12944301... | lld:pubmed |
| pubmed-article:12944301 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12944301 | pubmed:articleTitle | Mechanism of fluorescence and conformational changes of the sarcoplasmic calcium binding protein of the sand worm Nereis diversicolor upon Ca2+ or Mg2+ binding. | lld:pubmed |
| pubmed-article:12944301 | pubmed:affiliation | Laboratory of Biomolecular Dynamics, Catholic University of Leuven, Belgium. | lld:pubmed |
| pubmed-article:12944301 | pubmed:publicationType | Journal Article | lld:pubmed |
