{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T19:21:46Z","timestamp":1790623306073,"version":"4.1.0"},"reference-count":62,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":5174,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1994,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The backbone resonance assignments have been completed for the apo (<jats:sup>1<\/jats:sup>H and <jats:sup>15<\/jats:sup>N) and calcium\u2010loaded (<jats:sup>1<\/jats:sup>H, <jats:sup>15<\/jats:sup>N, and <jats:sup>13<\/jats:sup>C) regulatory N\u2010domain of chicken skeletal troponin\u2010C (1\u201390), using multidimensional homonuclear and heteronuclear NMR spectroscopy. The chemical\u2010shift information, along with detailed NOE analysis and <jats:sup>3<\/jats:sup><jats:italic>J<\/jats:italic><jats:sub>HNH\u03b1<\/jats:sub> coupling constants, permitted the determination and quantification of the Ca<jats:sup>2+<\/jats:sup>\u2010induced secondary structural change in the N\u2010domain of TnC. For both structures, 5 helices and 2 short \u03b2\u2010strands were found, as was observed in the apo N\u2010domain of the crystal structure of whole TnC (Herzberg O, James MNG, 1988, <jats:italic>J Mol Biol 203<\/jats:italic>:761\u2013779). The NMR solution structure of the apo form is indistinguishable from the crystal structure, whereas some structural differences are evident when comparing the 2Ca<jats:sup>2+<\/jats:sup> state solution structure with the apo one. The major conformational change observed is the straightening of helix\u2010B upon Ca<jats:sup>2+<\/jats:sup> binding. The possible importance and role of this conformational change is explored. Previous CD studies on the regulatory domain of TnC showed a significant Ca<jats:sup>2+<\/jats:sup>\u2010induced increase in negative ellipticity, suggesting a significant increase in helical content upon Ca<jats:sup>2+<\/jats:sup> binding. The present study shows that there is virtually no change in \u03b1\u2010helical content associated with the transition from apo to the 2Ca<jats:sup>2+<\/jats:sup> state of the N\u2010domain of TnC. Therefore, the Ca<jats:sup>2+<\/jats:sup>\u2010induced increase in ellipticity observed by CD does not relate to a change in helical content, but more likely to changes in spatial orientation of helices.<\/jats:p>","DOI":"10.1002\/pro.5560031108","type":"journal-article","created":{"date-parts":[[2009,2,10]],"date-time":"2009-02-10T01:25:33Z","timestamp":1234229133000},"page":"1961-1974","source":"Crossref","is-referenced-by-count":127,"title":["Quantification of the calcium\u2010induced secondary structural changes in the regulatory domain of troponin\u2010C"],"prefix":"10.1002","volume":"3","author":[{"given":"St\u00e9phane M.","family":"Gagn\u00e9","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sakae","family":"Tsuda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Monica 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