| pubmed-article:21098298 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C0033164 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C0043047 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C1948066 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C0002716 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C0205222 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C0005978 | lld:lifeskim |
| pubmed-article:21098298 | lifeskim:mentions | umls-concept:C0127400 | lld:lifeskim |
| pubmed-article:21098298 | pubmed:issue | 50 | lld:pubmed |
| pubmed-article:21098298 | pubmed:dateCreated | 2011-3-22 | lld:pubmed |
| pubmed-article:21098298 | pubmed:abstractText | Amyloid-like fibrils from a number of small peptides that are unrelated by sequence adopt a cross-?-spine in which the two sheets fully interdigitate to create a dry interface. Formation of such a dry interface is usually associated with self-assembly of extended hydrophobic surfaces. Here we investigate how a dry interface is created in the process of protofilament formation in vastly different sequences using two amyloidogenic peptides, one a polar sequence from the N terminus of the yeast prion Sup35 and the other a predominantly hydrophobic sequence from the C terminus of A?-peptide. Using molecular dynamics simulations with three force fields we show that spontaneous formation of two ordered one-dimensional water wires in the pore between the two sheets of the Sup35 protofilaments results in long-lived structures, which are stabilized by a network of hydrogen bonds between the water molecules in the wires and the polar side chains in the ?-sheet. Upon decreasing the stability of the metastable structures, water molecules are expelled resulting in a helically twisted protofilament in which side chains from a pair of ?-strands in each sheet pack perfectly resulting in a dry interface. Although drying in hydrophobically dominated interfaces is abrupt, resembling a liquid to vapor transition, we find that discrete transitions between the liquid to one-dimensional ordered water in the nanopore enclosed by the two ?-sheets to dry interface formation characterizes protofilament assembly in the yeast prions. Indeed, as the two sheets of the hydrophobic A?-sequence approach each other, fibril formation and expulsion of water molecules occur rapidly and nearly simultaneously. | lld:pubmed |
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| pubmed-article:21098298 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21098298 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21098298 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21098298 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21098298 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:21098298 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21098298 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21098298 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:21098298 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:21098298 | pubmed:author | pubmed-author:ThirumalaiDD | lld:pubmed |
| pubmed-article:21098298 | pubmed:author | pubmed-author:StraubJohn... | lld:pubmed |
| pubmed-article:21098298 | pubmed:author | pubmed-author:ReddyGovardha... | lld:pubmed |
| pubmed-article:21098298 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21098298 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:21098298 | pubmed:volume | 107 | lld:pubmed |
| pubmed-article:21098298 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21098298 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21098298 | pubmed:pagination | 21459-64 | lld:pubmed |
| pubmed-article:21098298 | pubmed:dateRevised | 2011-8-1 | lld:pubmed |
| pubmed-article:21098298 | pubmed:meshHeading | pubmed-meshheading:21098298... | lld:pubmed |
| pubmed-article:21098298 | pubmed:meshHeading | pubmed-meshheading:21098298... | lld:pubmed |
| pubmed-article:21098298 | pubmed:meshHeading | pubmed-meshheading:21098298... | lld:pubmed |
| pubmed-article:21098298 | pubmed:meshHeading | pubmed-meshheading:21098298... | lld:pubmed |
| pubmed-article:21098298 | pubmed:meshHeading | pubmed-meshheading:21098298... | lld:pubmed |
| pubmed-article:21098298 | pubmed:meshHeading | pubmed-meshheading:21098298... | lld:pubmed |
| pubmed-article:21098298 | pubmed:meshHeading | pubmed-meshheading:21098298... | lld:pubmed |
| pubmed-article:21098298 | pubmed:meshHeading | pubmed-meshheading:21098298... | lld:pubmed |
| pubmed-article:21098298 | pubmed:meshHeading | pubmed-meshheading:21098298... | lld:pubmed |
| pubmed-article:21098298 | pubmed:meshHeading | pubmed-meshheading:21098298... | lld:pubmed |
| pubmed-article:21098298 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:21098298 | pubmed:articleTitle | Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires. | lld:pubmed |
| pubmed-article:21098298 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Maryland, Biophysics Program, Institute for Physical Science and Technology, College Park, MD 20742, USA. | lld:pubmed |
| pubmed-article:21098298 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21098298 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:21098298 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:21098298 | lld:pubmed |
