{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T20:41:08Z","timestamp":1767991268548,"version":"3.49.0"},"reference-count":56,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":4932,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1995,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The solution secondary structure of calcium\u2010saturated skeletal troponin C (TnC) in the presence of 15% (v\/v) trifluoroethanol (TFE), which has been shown to exist predominantly as a monomer (Slupsky CM, Kay CM, Reinach FC, Smillie LB, Sykes BD, 1995, <jats:italic>Biochemistry 34<\/jats:italic>, forthcoming), has been investigated using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The <jats:sup>1<\/jats:sup>H, <jats:sup>15<\/jats:sup>N, and <jats:sup>13<\/jats:sup>C NMR chemical shift values for TnC in the presence of TFE are very similar to values obtained for calcium\u2010saturated NTnC (residues 1\u201390 of skeletal TnC), calmodulin, and synthetic peptide homodimers. Moreover, the secondary structure elements of TnC are virtually identical to those obtained for calcium\u2010saturated NTnC, calmodulin, and the synthetic peptide homodimers, suggesting that 15% (v\/v) TFE minimally perturbs the secondary and tertiary structure of this stably folded protein. Comparison of the solution structure of calcium\u2010saturated TnC with the X\u2010ray crystal structure of half\u2010saturated TnC reveals differences in the \u03d5\/\u03a8 angles of residue Glu 41 and in the linker between the two domains. Glu 41 has irregular \u03d5\/\u03a8 angles in the crystal structure, producing a kink in the B helix, whereas in calcium\u2010saturated TnC, Glu 41 has helical \u03d5\/\u03a8 angles, resulting in a straight B helix. The linker between the N and C domains of calcium\u2010saturated TnC is flexible in the solution structure.<\/jats:p>","DOI":"10.1002\/pro.5560040704","type":"journal-article","created":{"date-parts":[[2009,2,10]],"date-time":"2009-02-10T02:47:07Z","timestamp":1234234027000},"page":"1279-1290","source":"Crossref","is-referenced-by-count":23,"title":["Solution secondary structure of calcium\u2010saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy"],"prefix":"10.1002","volume":"4","author":[{"given":"Carolyn M.","family":"Slupsky","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lawrence B.","family":"Smillie","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Brian D.","family":"Sykes","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fernando C.","family":"Reinach","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"crossref","first-page":"19232","DOI":"10.1016\/S0021-9258(19)36504-4","article-title":"Critical minimum length of the central helix in troponin C for the Ca2+ switch in muscular contraction","volume":"268","author":"Babu A","year":"1993","journal-title":"J Biol Chem"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00138a005"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2364(90)90320-9"},{"key":"e_1_2_1_5_1","first-page":"174","article-title":"Removal of F1 baseline distortion and optimization of folding in multidimensional NMR spectra","volume":"91","author":"Bax A","year":"1990","journal-title":"J Magn Reson"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/0009-2614(80)80041-8"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.2047852"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00243a008"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2795(80)90003-3"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1038\/345182a0"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560031108"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2364(91)90341-P"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmra.1993.1099"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1038\/345132a0"},{"key":"e_1_2_1_15_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF01738034"},{"key":"e_1_2_1_16_1","doi-asserted-by":"publisher","DOI":"10.1002\/prot.340190402"},{"key":"e_1_2_1_17_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2364(92)90099-S"},{"key":"e_1_2_1_18_1","doi-asserted-by":"crossref","first-page":"11685","DOI":"10.1016\/S0021-9258(19)50254-X","article-title":"Identification of regions conferring calmodulin\u2010like properties to troponin C","volume":"268","author":"Gulati J","year":"1993","journal-title":"J Biol Chem"},{"key":"e_1_2_1_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(90)81409-H"},{"key":"e_1_2_1_20_1","doi-asserted-by":"crossref","first-page":"16622","DOI":"10.1016\/S0021-9258(18)55346-1","article-title":"Stabilization by a disulfide bond of the N\u2010terminal domain of a mutant troponin C (TnC48\/82)","volume":"266","author":"Gusev NB","year":"1991","journal-title":"J Biol Chem"},{"key":"e_1_2_1_21_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00403a011"},{"key":"e_1_2_1_22_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(88)90208-2"},{"key":"e_1_2_1_23_1","doi-asserted-by":"crossref","first-page":"2638","DOI":"10.1016\/S0021-9258(17)35835-0","article-title":"A model for the Ca2+ induced conformational transition of troponin C","volume":"261","author":"Herzberg O","year":"1986","journal-title":"J Biol Chem"},{"key":"e_1_2_1_24_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00471a022"},{"key":"e_1_2_1_25_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2364(90)90227-Z"},{"key":"e_1_2_1_26_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00102a013"},{"key":"e_1_2_1_27_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2364(90)90215-U"},{"key":"e_1_2_1_28_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00231a031"},{"key":"e_1_2_1_29_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2364(89)90006-1"},{"key":"e_1_2_1_30_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(77)90113-9"},{"key":"e_1_2_1_31_1","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2795(78)90028-4"},{"key":"e_1_2_1_32_1","doi-asserted-by":"crossref","unstructured":"LiMX Gagn\u00e9SM TsudaS KayCM SmillieLB SykesBD.1995.Calcium binding to the regulatory N domain of skeletal muscle troponin C occurs in a step\u2010wise manner.Biochemistry. 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