| pubmed-article:7723032 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7723032 | lifeskim:mentions | umls-concept:C0043047 | lld:lifeskim |
| pubmed-article:7723032 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:7723032 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
| pubmed-article:7723032 | lifeskim:mentions | umls-concept:C0001963 | lld:lifeskim |
| pubmed-article:7723032 | lifeskim:mentions | umls-concept:C0008238 | lld:lifeskim |
| pubmed-article:7723032 | lifeskim:mentions | umls-concept:C0014406 | lld:lifeskim |
| pubmed-article:7723032 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:7723032 | lifeskim:mentions | umls-concept:C1442758 | lld:lifeskim |
| pubmed-article:7723032 | lifeskim:mentions | umls-concept:C2717775 | lld:lifeskim |
| pubmed-article:7723032 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:7723032 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:7723032 | pubmed:dateCreated | 1995-5-25 | lld:pubmed |
| pubmed-article:7723032 | pubmed:abstractText | A series of three molecular dynamics simulations at 300 K in explicit solvent environments of chloroform, methanol and water has been performed on the pulmonary surfactant lipoprotein, SP-C, comprising several consecutive valine residues in order to investigate the stability of the alpha-helical conformation. Two additional simulations were performed on truncated SP-C with a five-residue N-terminal deletion at 300 K and 500 K in water, the high temperature run in order to increase the rate of peptide denaturation. Indications of destabilization appear in chloroform during 1 ns while the SP-C alpha-helix is remarkably stable during 1 ns in methanol and water. In particular the polyvalyl part comprising residues Val15 to Val21 remains intact even at elevated temperature, and the valines do not disrupt the alpha-helical conformation. The valyl-rotamer sampling is partly restricted. Unfolding takes place successively along the primary sequence starting from the C-terminal end. Factors affecting polypeptide stability in molecular dynamics simulations are addressed. The intrinsic helix-forming tendency of valine residues and its dependence on the sequence context, and the role of the solvent environment in stabilizing or destabilizing an alpha-helical fold, are discussed. | lld:pubmed |
| pubmed-article:7723032 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7723032 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7723032 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7723032 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7723032 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7723032 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:7723032 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:7723032 | pubmed:author | pubmed-author:JohanssonJJ | lld:pubmed |
| pubmed-article:7723032 | pubmed:author | pubmed-author:MarkA EAE | lld:pubmed |
| pubmed-article:7723032 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:7723032 | pubmed:author | pubmed-author:KovacsHH | lld:pubmed |
| pubmed-article:7723032 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7723032 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:7723032 | pubmed:volume | 247 | lld:pubmed |
| pubmed-article:7723032 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7723032 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7723032 | pubmed:pagination | 808-22 | lld:pubmed |
| pubmed-article:7723032 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7723032 | pubmed:meshHeading | pubmed-meshheading:7723032-... | lld:pubmed |
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| pubmed-article:7723032 | pubmed:meshHeading | pubmed-meshheading:7723032-... | lld:pubmed |
| pubmed-article:7723032 | pubmed:meshHeading | pubmed-meshheading:7723032-... | lld:pubmed |
| pubmed-article:7723032 | pubmed:meshHeading | pubmed-meshheading:7723032-... | lld:pubmed |
| pubmed-article:7723032 | pubmed:meshHeading | pubmed-meshheading:7723032-... | lld:pubmed |
| pubmed-article:7723032 | pubmed:meshHeading | pubmed-meshheading:7723032-... | lld:pubmed |
| pubmed-article:7723032 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7723032 | pubmed:articleTitle | The effect of environment on the stability of an integral membrane helix: molecular dynamics simulations of surfactant protein C in chloroform, methanol and water. | lld:pubmed |
| pubmed-article:7723032 | pubmed:affiliation | Laboratory of Physical Chemistry, ETH-Zentrum CH-8092, Zürich, Switzerland. | lld:pubmed |
| pubmed-article:7723032 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7723032 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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