| pubmed-article:10233063 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10233063 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:10233063 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:10233063 | lifeskim:mentions | umls-concept:C0037638 | lld:lifeskim |
| pubmed-article:10233063 | lifeskim:mentions | umls-concept:C0679083 | lld:lifeskim |
| pubmed-article:10233063 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10233063 | pubmed:dateCreated | 1999-6-21 | lld:pubmed |
| pubmed-article:10233063 | pubmed:abstractText | We describe application of the implicit solvation model (see the first paper of this series), to Monte Carlo simulations of several peptides in bilayer- and water-mimetic environments, and in vacuum. The membrane-bound peptides chosen were transmembrane segments A and B of bacteriorhodopsin, the hydrophobic segment of surfactant lipoprotein, and magainin2. Their conformations in membrane-like media are known from the experiments. Also, molecular dynamics study of surfactant lipoprotein with different explicit solvents has been reported (Kovacs, H., A. E. Mark, J. Johansson, and W. F. van Gunsteren. 1995. J. Mol. Biol. 247:808-822). The principal goal of this work is to compare the results obtained in the framework of our solvation model with available experimental and computational data. The findings could be summarized as follows: 1) structural and energetic properties of studied molecules strongly depend on the solvent; membrane-mimetic media significantly promote formation of alpha-helices capable of traversing the bilayer, whereas a polar environment destabilizes alpha-helical conformation via reduction of solvent-exposed surface area and packing; 2) the structures calculated in a membrane-like environment agree with the experimental ones; 3) noticeable differences in conformation of surfactant lipoprotein assessed via Monte Carlo simulation with implicit solvent (this work) and molecular dynamics in explicit solvent were observed; 4) in vacuo simulations do not correctly reproduce protein-membrane interactions, and hence should be avoided in modeling membrane proteins. | lld:pubmed |
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| pubmed-article:10233063 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10233063 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10233063 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10233063 | pubmed:month | May | lld:pubmed |
| pubmed-article:10233063 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:10233063 | pubmed:author | pubmed-author:ArsenievA SAS | lld:pubmed |
| pubmed-article:10233063 | pubmed:author | pubmed-author:VergotenGG | lld:pubmed |
| pubmed-article:10233063 | pubmed:author | pubmed-author:EfremovR GRG | lld:pubmed |
| pubmed-article:10233063 | pubmed:author | pubmed-author:NoldeD EDE | lld:pubmed |
| pubmed-article:10233063 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10233063 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:10233063 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10233063 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10233063 | pubmed:pagination | 2460-71 | lld:pubmed |
| pubmed-article:10233063 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:10233063 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10233063 | pubmed:articleTitle | A solvent model for simulations of peptides in bilayers. II. Membrane-spanning alpha-helices. | lld:pubmed |
| pubmed-article:10233063 | pubmed:affiliation | M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya, 16/10, Moscow V-437, 117871 GSP, Russia. efremov@nmr.ru | lld:pubmed |
| pubmed-article:10233063 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10233063 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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