| pubmed-article:2768217 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2768217 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:2768217 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:2768217 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:2768217 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:2768217 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2768217 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:2768217 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:2768217 | lifeskim:mentions | umls-concept:C0205372 | lld:lifeskim |
| pubmed-article:2768217 | lifeskim:mentions | umls-concept:C0065739 | lld:lifeskim |
| pubmed-article:2768217 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:2768217 | pubmed:dateCreated | 1989-10-10 | lld:pubmed |
| pubmed-article:2768217 | pubmed:abstractText | The technique of small-angle X-ray scattering has been employed to examine the solution conformation of calmodulin and its complexes with Ca2+ alone, and with both Ca2+ and mastoparan. The radius of gyration decreased by 3.1 +/- 0.3 A upon binding of both 4 mol Ca2+/mol of protein and 1 mol mastoparan/mol of protein to form the ternary complex. A smaller increase was found for the separate binding of 4 mol Ca2+/mol of protein in the absence of mastoparan (0.6 +/- 0.3 A). The analyses of pair distance distribution function showed that the maximal pair distance in calmodulin complex with both Ca2+ and mastoparan decreased by 20-30% in comparison with calmodulin or its complex with Ca2+, and a shoulder near 40 A, which characterizes the dumbbell-shaped molecule of calmodulin, disappeared. These results indicate that the two globular domains of the calmodulin complex with Ca2+ and mastoparan come close together by 8.0-9.5 A on average, if the size and the overall shape of the globular domains are the same in Ca2+-calmodulin-mastoparan complex as in calmodulin or Ca2+-calmodulin complex. | lld:pubmed |
| pubmed-article:2768217 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2768217 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2768217 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2768217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2768217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2768217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2768217 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2768217 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2768217 | pubmed:issn | 0021-924X | lld:pubmed |
| pubmed-article:2768217 | pubmed:author | pubmed-author:MiyakeYY | lld:pubmed |
| pubmed-article:2768217 | pubmed:author | pubmed-author:MatsuoTT | lld:pubmed |
| pubmed-article:2768217 | pubmed:author | pubmed-author:IzumiYY | lld:pubmed |
| pubmed-article:2768217 | pubmed:author | pubmed-author:UekiTT | lld:pubmed |
| pubmed-article:2768217 | pubmed:author | pubmed-author:YoshinoHH | lld:pubmed |
| pubmed-article:2768217 | pubmed:author | pubmed-author:MatsushimaNN | lld:pubmed |
| pubmed-article:2768217 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2768217 | pubmed:volume | 105 | lld:pubmed |
| pubmed-article:2768217 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2768217 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2768217 | pubmed:pagination | 883-7 | lld:pubmed |
| pubmed-article:2768217 | pubmed:dateRevised | 2007-12-19 | lld:pubmed |
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| pubmed-article:2768217 | pubmed:meshHeading | pubmed-meshheading:2768217-... | lld:pubmed |
| pubmed-article:2768217 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2768217 | pubmed:articleTitle | Binding of both Ca2+ and mastoparan to calmodulin induces a large change in the tertiary structure. | lld:pubmed |
| pubmed-article:2768217 | pubmed:affiliation | School of Allied Health Professions, Sapporo Medical College, Hokkaido. | lld:pubmed |
| pubmed-article:2768217 | pubmed:publicationType | Journal Article | lld:pubmed |
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