On the role of structural class of a protein with two-state folding kinetics in determining correlations between its size, topology, and folding rate.

ABSTRACT: The time it takes for proteins to fold into their native states varies over several orders of magnitude depending on their native-state topology, size, and amino acid composition. In a number of previous studies, it was found that there is strong correlation between logarithmic folding rates and contact order for proteins that fold with two-state kinetics, while such correlation is absent for three-state proteins. Conversely, strong correlations between folding rates and chain length occur within three-state proteins, but not in two-state proteins. Here, we demonstrate that chain lengths and folding rates of two-state proteins are not correlated with each other only when all-alpha, all-beta, and mixed-class proteins are considered together, which is typically the case. However, when consid

SUBMITTER: Istomin AY 

PROVIDER: S-EPMC2211710 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature