Ensemble of transition states for two-state protein folding from the eigenvectors of rate matrices

The transition state ensemble from the eigenvectors of a rate matrix that describes the interconversion of microstates during the folding of a two-state protein was investigated. The first eigenvalue, which corresponds to the equilibrium distribution, is zero, λ 1 = 0 and the rest are negative. A distinctive feature of two-state proteins is the presence of a gap in the eigenvalue spectrum. It is stated that the procedure for finding the transition state ensemble will be used to analyze the microscopic kinetics models of two-state protein folding and will lead to meaningful insights into the underlying mechanism of the folding.