| pubmed-article:17596847 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17596847 | lifeskim:mentions | umls-concept:C0026339 | lld:lifeskim |
| pubmed-article:17596847 | lifeskim:mentions | umls-concept:C1882071 | lld:lifeskim |
| pubmed-article:17596847 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:17596847 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:17596847 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
| pubmed-article:17596847 | lifeskim:mentions | umls-concept:C0205430 | lld:lifeskim |
| pubmed-article:17596847 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
| pubmed-article:17596847 | lifeskim:mentions | umls-concept:C0681018 | lld:lifeskim |
| pubmed-article:17596847 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17596847 | pubmed:dateCreated | 2007-8-28 | lld:pubmed |
| pubmed-article:17596847 | pubmed:abstractText | We develop a mixed elastic network model (MENM) to study large-scale conformational transitions of proteins between two (or more) known structures. Elastic network potentials for the beginning and end states of a transition are combined, in effect, by adding their respective partition functions. The resulting effective MENM energy function smoothly interpolates between the original surfaces, and retains the beginning and end structures as local minima. Saddle points, transition paths, potentials of mean force, and partition functions can be found efficiently by largely analytic methods. To characterize the protein motions during a conformational transition, we follow "transition paths" on the MENM surface that connect the beginning and end structures and are invariant to parameterizations of the model and the mathematical form of the mixing scheme. As illustrations of the general formalism, we study large-scale conformation changes of the motor proteins KIF1A kinesin and myosin II. We generate possible transition paths for these two proteins that reveal details of their conformational motions. The MENM formalism is computationally efficient and generally applicable even for large protein systems that undergo highly collective structural changes. | lld:pubmed |
| pubmed-article:17596847 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17596847 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17596847 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17596847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17596847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17596847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17596847 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17596847 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17596847 | pubmed:issn | 1097-0134 | lld:pubmed |
| pubmed-article:17596847 | pubmed:author | pubmed-author:ZhengWenjunW | lld:pubmed |
| pubmed-article:17596847 | pubmed:author | pubmed-author:HummerGerhard... | lld:pubmed |
| pubmed-article:17596847 | pubmed:author | pubmed-author:BrooksBernard... | lld:pubmed |
| pubmed-article:17596847 | pubmed:copyrightInfo | 2007 Wiley-Liss, Inc. | lld:pubmed |
| pubmed-article:17596847 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17596847 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17596847 | pubmed:volume | 69 | lld:pubmed |
| pubmed-article:17596847 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17596847 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17596847 | pubmed:pagination | 43-57 | lld:pubmed |
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| pubmed-article:17596847 | pubmed:meshHeading | pubmed-meshheading:17596847... | lld:pubmed |
| pubmed-article:17596847 | pubmed:meshHeading | pubmed-meshheading:17596847... | lld:pubmed |
| pubmed-article:17596847 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17596847 | pubmed:articleTitle | Protein conformational transitions explored by mixed elastic network models. | lld:pubmed |
| pubmed-article:17596847 | pubmed:affiliation | Laboratory of Computational Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA. | lld:pubmed |
| pubmed-article:17596847 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17596847 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| pubmed-article:17596847 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
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