title: Do prokaryotes have more kinetically stable proteins than eukaryotic organisms?
abstract: 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.
authors.affiliation: Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, 110 8th Street, Troy, New York 12180, USA.
authors.forename: Ke
authors.initials: K
authors.lastname: Xia
authors.forename: Songjie
authors.initials: S
authors.lastname: Zhang
authors.forename: Brent A
authors.initials: BA
authors.lastname: Solina
authors.forename: Blanca
authors.initials: B
authors.lastname: Barquera
authors.forename: Wilfredo
authors.initials: W
authors.lastname: Colón
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D056890:Eukaryota; D011387:Prokaryotic Cells; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*
chemical_list: D011506:Proteins