| pubmed-article:18665616 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18665616 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:18665616 | lifeskim:mentions | umls-concept:C0010383 | lld:lifeskim |
| pubmed-article:18665616 | lifeskim:mentions | umls-concept:C0332621 | lld:lifeskim |
| pubmed-article:18665616 | pubmed:issue | 34 | lld:pubmed |
| pubmed-article:18665616 | pubmed:dateCreated | 2008-8-19 | lld:pubmed |
| pubmed-article:18665616 | pubmed:abstractText | Macromolecular crowding is expected to have a significant effect on protein aggregation. In the present study we analyzed the effect of macromolecular crowding on fibrillation of four proteins, bovine S-carboxymethyl-alpha-lactalbumin (a disordered form of the protein with reduced three out of four disulfide bridges), human insulin, bovine core histones, and human alpha-synuclein. These proteins are structurally different, varying from natively unfolded (alpha-synuclein and core histones) to folded proteins with rigid tertiary and quaternary structures (monomeric and hexameric forms of insulin). All these proteins are known to fibrillate in diluted solutions, however their aggregation mechanisms are very divers and some of them are able to form different aggregates in addition to fibrils. We studied how macromolecular crowding guides protein between different aggregation pathways by analyzing the effect of crowding agents on the aggregation patterns under the variety of conditions favoring different aggregated end products in diluted solutions. | lld:pubmed |
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