{"refrec":{"BRefID":281017,"RR":"<b>Sillen, A.; Verheyden, S.; Delfosse, L.; Braem, T.; Robben, J.; Volckaert, G.; Engelborghs, Y.</b> (2003). Mechanism of fluorescence and conformational changes of the sarcoplasmic calcium binding protein of the sand worm <i>Nereis diversicolor</i> upon Ca<sup>2+</sup> or Mg<sup>2+</sup> binding. <i>Biophys. J. 85(3)</i>: 1882-1893. <a href=\"https://dx.doi.org/10.1016/S0006-3495(03)74616-5\" target=\"_blank\">https://dx.doi.org/10.1016/S0006-3495(03)74616-5</a>","BEntID":273036,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Biophys. J. 85(3)</i>: 1882-1893. <a href=\"https://dx.doi.org/10.1016/S0006-3495(03)74616-5\" target=\"_blank\">https://dx.doi.org/10.1016/S0006-3495(03)74616-5</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Sillen, A.; Verheyden, S.; Delfosse, L.; Braem, T.; Robben, J.; Volckaert, G.; Engelborghs, Y.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Sillen, A. <i>et al.</i>","Englishabstract":"The calcium-binding protein isolated from the sarcoplasm of the muscles of the sand worm <i>Nereis diversicolor</i> has four EF-hands and three active binding sites for Ca<sup>2+</sup> or Mg<sup>2+</sup>. <i>Nereis diversicolor</i> 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<sup>2+</sup> or Mg<sup>2+</sup>. 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, <i>Trp</i>170 shows a strong fluorescence increase, <i>Trp</i>57 an extensive fluorescence decrease, and <i>Trp</i>4 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 <i>z</i>-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 <i>Trp</i>57 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.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Mechanism of fluorescence and conformational changes of the sarcoplasmic calcium binding protein of the sand worm <i>Nereis diversicolor</i> upon Ca<sup>2+</sup> or Mg<sup>2+</sup> binding","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-25 01:32:36.236382","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2003,"MonPub":null,"DateUpdate":"2022-07-08","DateCreate":"2016-10-09","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000185009900048","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/S0006-3495(03)74616-5"},"refs":null,"anarec":{"AnaID":281017,"PubliDate":2003,"Pagination":"1882-1893","XtraPublOfAnaID":null,"ISBN":null,"Volume":"85","Issue":"3","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42267,"SerRR":"Biophysical Journal. 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