| pubmed-article:11340656 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11340656 | lifeskim:mentions | umls-concept:C0681916 | lld:lifeskim |
| pubmed-article:11340656 | lifeskim:mentions | umls-concept:C0750572 | lld:lifeskim |
| pubmed-article:11340656 | lifeskim:mentions | umls-concept:C0678591 | lld:lifeskim |
| pubmed-article:11340656 | lifeskim:mentions | umls-concept:C0680844 | lld:lifeskim |
| pubmed-article:11340656 | lifeskim:mentions | umls-concept:C0071642 | lld:lifeskim |
| pubmed-article:11340656 | lifeskim:mentions | umls-concept:C0173022 | lld:lifeskim |
| pubmed-article:11340656 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:11340656 | pubmed:dateCreated | 2001-5-7 | lld:pubmed |
| pubmed-article:11340656 | pubmed:abstractText | Molecular dynamics simulations were conducted to estimate the free energy barrier of unfolding surfactant-associated polypeptide C (SP-C) from an alpha-helical conformation. Experimental studies indicate that while the helical fold of SP-C is thermodynamically stable in phospholipid micelles, it is metastable in a mixed organic solvent of CHCl3/CH3OH/0.1 M HCl at 32:64:5 (v/v/v), in which it undergoes an irreversible transformation to an insoluble aggregate that contains beta-sheet. On the basis of experimental observations, the free energy barrier was estimated to be approximately 100 kJ/mole by applying Eyring's transition state theory to the experimental rate of unfolding [Protein Sci 1998;7:2533-2540]. These studies prompted us to carry out simulations to investigate the unwinding process of two helical turns encompassing residues 25-32 in water and in methanol. The results give an upper bound estimation for the free energy barrier of unfolding of SP-C of approximately 20 kJ/mole. The results suggest a need to reconsider the applicability of a single-mode activated process theory to protein unfolding. | lld:pubmed |
| pubmed-article:11340656 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11340656 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11340656 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11340656 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11340656 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11340656 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11340656 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11340656 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11340656 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11340656 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:11340656 | pubmed:issn | 0887-3585 | lld:pubmed |
| pubmed-article:11340656 | pubmed:author | pubmed-author:JohanssonJJ | lld:pubmed |
| pubmed-article:11340656 | pubmed:author | pubmed-author:MarkA EAE | lld:pubmed |
| pubmed-article:11340656 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:11340656 | pubmed:author | pubmed-author:KovacsHH | lld:pubmed |
| pubmed-article:11340656 | pubmed:author | pubmed-author:ZanglWW | lld:pubmed |
| pubmed-article:11340656 | pubmed:copyrightInfo | Copyright 2001 Wiley-Liss, Inc. | lld:pubmed |
| pubmed-article:11340656 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11340656 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11340656 | pubmed:volume | 43 | lld:pubmed |
| pubmed-article:11340656 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11340656 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11340656 | pubmed:pagination | 395-402 | lld:pubmed |
| pubmed-article:11340656 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:meshHeading | pubmed-meshheading:11340656... | lld:pubmed |
| pubmed-article:11340656 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11340656 | pubmed:articleTitle | Free energy barrier estimation of unfolding the alpha-helical surfactant-associated polypeptide C. | lld:pubmed |
| pubmed-article:11340656 | pubmed:affiliation | Groningen Biomolecular Sciences and Biotechnology Institute, Department of Biophysical Chemistry, University of Groningen, Groningen, The Netherlands. | lld:pubmed |
| pubmed-article:11340656 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11340656 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11340656 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11340656 | lld:pubmed |
