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