| pubmed-article:9923699 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9923699 | lifeskim:mentions | umls-concept:C0077400 | lld:lifeskim |
| pubmed-article:9923699 | lifeskim:mentions | umls-concept:C0205143 | lld:lifeskim |
| pubmed-article:9923699 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:9923699 | pubmed:issue | 2-3 | lld:pubmed |
| pubmed-article:9923699 | pubmed:dateCreated | 1999-4-22 | lld:pubmed |
| pubmed-article:9923699 | pubmed:abstractText | The calcium-induced structural changes in the skeletal muscle regulatory protein troponin C involve a transition from a closed to an open structure with the concomitant exposure of a large hydrophobic interaction site for target proteins. NMR solution structural studies have served to define this conformational change and elucidate the mechanism of the linkage between calcium binding and the induced structural changes. These structural movements are described in terms of interhelical angles in these largely helical proteins. Oddly, the most recent structure of the cardiac system challenges the central paradigm because the calcium-bound structures are not open. The kinetics, energetics, and dynamics of these proteins have also been investigated using NMR. | lld:pubmed |
| pubmed-article:9923699 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9923699 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9923699 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9923699 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9923699 | pubmed:issn | 0829-8211 | lld:pubmed |
| pubmed-article:9923699 | pubmed:author | pubmed-author:SykesB DBD | lld:pubmed |
| pubmed-article:9923699 | pubmed:author | pubmed-author:LiM XMX | lld:pubmed |
| pubmed-article:9923699 | pubmed:author | pubmed-author:GagnéS MSM | lld:pubmed |
| pubmed-article:9923699 | pubmed:author | pubmed-author:McKayR TRT | lld:pubmed |
| pubmed-article:9923699 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9923699 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:9923699 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9923699 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9923699 | pubmed:pagination | 302-12 | lld:pubmed |
| pubmed-article:9923699 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:9923699 | pubmed:meshHeading | pubmed-meshheading:9923699-... | lld:pubmed |
| pubmed-article:9923699 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9923699 | pubmed:articleTitle | The NMR angle on troponin C. | lld:pubmed |
| pubmed-article:9923699 | pubmed:affiliation | Department of Biochemistry, University of Alberta, Edmonton, Canada. | lld:pubmed |
| pubmed-article:9923699 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9923699 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:9923699 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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