| pubmed-article:19518258 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19518258 | lifeskim:mentions | umls-concept:C0015498 | lld:lifeskim |
| pubmed-article:19518258 | lifeskim:mentions | umls-concept:C1511359 | lld:lifeskim |
| pubmed-article:19518258 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:19518258 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:19518258 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:19518258 | lifeskim:mentions | umls-concept:C1705483 | lld:lifeskim |
| pubmed-article:19518258 | lifeskim:mentions | umls-concept:C0587267 | lld:lifeskim |
| pubmed-article:19518258 | pubmed:issue | 4 Pt 1 | lld:pubmed |
| pubmed-article:19518258 | pubmed:dateCreated | 2009-6-12 | lld:pubmed |
| pubmed-article:19518258 | pubmed:abstractText | We test a hypothesis that the closed form of the C2 domain of coagulation factor V is more stable than the open form in an aqueous environment using a two-dimensional free-energy calculation with a simple dielectric solvent model. Our result shows that while the free-energy difference between two forms is small, favoring the closed form, a two-dimensional free-energy surface (FES) reveals that a transition state (1.53 kcal/mol) exists between the two conformations. By mapping the one-dimensional order parameter DeltaQ onto the two-dimensional FES, we search the conformational change path with the highest Boltzmann weighting factor between the closed and open form of the factor V C2 domain. The predicted transition path from the closed to open form is not that of simple side chain movements, but instead concerted movements of several loops. We also present a one-dimensional free-energy profile using a collective order parameter, which in a coarse manner locates the energy barriers found on the two-dimensional FES. | lld:pubmed |
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| pubmed-article:19518258 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19518258 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19518258 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19518258 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19518258 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19518258 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19518258 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:19518258 | pubmed:issn | 1539-3755 | lld:pubmed |
| pubmed-article:19518258 | pubmed:author | pubmed-author:PedersenLee... | lld:pubmed |
| pubmed-article:19518258 | pubmed:author | pubmed-author:LeeChang... | lld:pubmed |
| pubmed-article:19518258 | pubmed:author | pubmed-author:WuSangwookS | lld:pubmed |
| pubmed-article:19518258 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19518258 | pubmed:volume | 79 | lld:pubmed |
| pubmed-article:19518258 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19518258 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19518258 | pubmed:pagination | 041909 | lld:pubmed |
| pubmed-article:19518258 | pubmed:dateRevised | 2010-9-27 | lld:pubmed |
| pubmed-article:19518258 | pubmed:meshHeading | pubmed-meshheading:19518258... | lld:pubmed |
| pubmed-article:19518258 | pubmed:meshHeading | pubmed-meshheading:19518258... | lld:pubmed |
| pubmed-article:19518258 | pubmed:meshHeading | pubmed-meshheading:19518258... | lld:pubmed |
| pubmed-article:19518258 | pubmed:meshHeading | pubmed-meshheading:19518258... | lld:pubmed |
| pubmed-article:19518258 | pubmed:meshHeading | pubmed-meshheading:19518258... | lld:pubmed |
| pubmed-article:19518258 | pubmed:meshHeading | pubmed-meshheading:19518258... | lld:pubmed |
| pubmed-article:19518258 | pubmed:meshHeading | pubmed-meshheading:19518258... | lld:pubmed |
| pubmed-article:19518258 | pubmed:meshHeading | pubmed-meshheading:19518258... | lld:pubmed |
| pubmed-article:19518258 | pubmed:meshHeading | pubmed-meshheading:19518258... | lld:pubmed |
| pubmed-article:19518258 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19518258 | pubmed:articleTitle | Conformational change path between closed and open forms of C2 domain of coagulation factor V on a two-dimensional free-energy surface. | lld:pubmed |
| pubmed-article:19518258 | pubmed:affiliation | Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-3290, USA. | lld:pubmed |
| pubmed-article:19518258 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19518258 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
