| Do prokaryotes have more kinetically stable proteins than eukaryotic organisms? | |
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MedLine Citation:
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PMID: 20677776 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Upon folding, some proteins become conformationally trapped, presumably to protect against aggregation or premature degradation. To probe the occurrence of this property, known as kinetic stability, we used a diagonal two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis method to probe biologically diverse organisms. The results show that kinetic stability is prevalent in prokaryotes, especially thermophiles, but uncommon in eukaryotic organisms, thereby suggesting that this property might be crucial for the adaptation and survival of less complex prokaryotic organisms. |
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Authors:
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Ke Xia; Songjie Zhang; Brent A Solina; Blanca Barquera; Wilfredo Colón |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Biochemistry Volume: 49 ISSN: 1520-4995 ISO Abbreviation: Biochemistry Publication Date: 2010 Aug |
Date Detail:
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Created Date: 2010-08-24 Completed Date: 2010-09-10 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: United States |
Other Details:
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Languages: eng Pagination: 7239-41 Citation Subset: IM |
Affiliation:
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Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, 110 8th Street, Troy, New York 12180, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Electrophoresis, Polyacrylamide Gel
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methods Eukaryota Prokaryotic Cells Proteins / chemistry*, genetics, isolation & purification* |
| Chemical | |
Reg. No./Substance:
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0/Proteins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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