rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2005-9-30
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pubmed:abstractText |
We introduce a novel approach to estimate differences in the beta-aggregation potential of eukaryotic proteomes. The approach is based on a statistical analysis of the beta-aggregation propensity of polypeptide segments, which is calculated by an equation derived from first principles using the physicochemical properties of the natural amino acids. Our analysis reveals a significant decreasing trend of the overall beta-aggregation tendency with increasing organism complexity and longevity. A comparison with randomized proteomes shows that natural proteomes have a higher degree of polarization in both low and high beta-aggregation prone sequences. The former originates from the requirement of intrinsically disordered proteins, whereas the latter originates from the necessity of proteins with a stable folded structure.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16155201-10470028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16155201-10679462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16155201-11050225,
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0961-8368
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2735-40
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16155201-Amino Acid Sequence,
pubmed-meshheading:16155201-Animals,
pubmed-meshheading:16155201-Databases, Protein,
pubmed-meshheading:16155201-Longevity,
pubmed-meshheading:16155201-Models, Molecular,
pubmed-meshheading:16155201-Protein Conformation,
pubmed-meshheading:16155201-Protein Denaturation,
pubmed-meshheading:16155201-Protein Folding,
pubmed-meshheading:16155201-Proteins,
pubmed-meshheading:16155201-Proteome
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pubmed:year |
2005
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pubmed:articleTitle |
Organism complexity anti-correlates with proteomic beta-aggregation propensity.
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pubmed:affiliation |
Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland. gian@bioc.unizh.ch
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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