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.