| pubmed-article:19167289 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19167289 | lifeskim:mentions | umls-concept:C0023821 | lld:lifeskim |
| pubmed-article:19167289 | lifeskim:mentions | umls-concept:C0085201 | lld:lifeskim |
| pubmed-article:19167289 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:19167289 | lifeskim:mentions | umls-concept:C0596957 | lld:lifeskim |
| pubmed-article:19167289 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:19167289 | pubmed:dateCreated | 2009-1-26 | lld:pubmed |
| pubmed-article:19167289 | pubmed:abstractText | Apolipoprotein (apo) A-I is an unusually flexible protein whose lipid-associated structure is poorly understood. Thermal denaturation, which is used to measure the global helix stability of high-density lipoprotein (HDL)-associated apoA-I, provides no information about local helix stability. Here we report the use of temperature jump molecular dynamics (MD) simulations to scan the per-residue helix stability of apoA-I in phospholipid-rich HDL. When three 20 ns MD simulations were performed at 500 K on each of two particles created by MD simulations at 310 K, bilayers remained intact but expanded by 40%, and total apoA-I helicity decreased from 95% to 72%. Of significance, the conformations of the overlapping N- and C-terminal domains of apoA-I in the particles were unusually mobile, exposing hydrocarbon regions of the phospholipid to solvent; a lack of buried interhelical salt bridges in the terminal domains correlated with increased mobility. Nondenaturing gradient gels show that 40% expansion of the phospholipid surface of 100:2 particles by addition of palmitoyloleoylphosphatidylcholine exceeds the threshold of particle stability. As a unifying hypothesis, we propose that the terminal domains of apoA-I are phospholipid concentration-sensitive molecular triggers for fusion/remodeling of HDL particles. Since HDL remodeling is necessary for cholesterol transport, our model for remodeling has substantial biomedical implications. | lld:pubmed |
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| pubmed-article:19167289 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19167289 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19167289 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19167289 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19167289 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19167289 | pubmed:issn | 1542-0086 | lld:pubmed |
| pubmed-article:19167289 | pubmed:author | pubmed-author:ChenJianguoJ | lld:pubmed |
| pubmed-article:19167289 | pubmed:author | pubmed-author:NgomN NNN | lld:pubmed |
| pubmed-article:19167289 | pubmed:author | pubmed-author:SegrestJere... | lld:pubmed |
| pubmed-article:19167289 | pubmed:author | pubmed-author:CatteAndreaA | lld:pubmed |
| pubmed-article:19167289 | pubmed:author | pubmed-author:PattersonJame... | lld:pubmed |
| pubmed-article:19167289 | pubmed:author | pubmed-author:GuFeifeiF | lld:pubmed |
| pubmed-article:19167289 | pubmed:author | pubmed-author:JonesMartin... | lld:pubmed |
| pubmed-article:19167289 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19167289 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:19167289 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19167289 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19167289 | pubmed:pagination | 354-71 | lld:pubmed |
| pubmed-article:19167289 | pubmed:dateRevised | 2010-9-22 | lld:pubmed |
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