RT Journal Article
T1 The protein folding transition state: Insights from kinetics and thermodynamics
A1 Travasso, Rui D.M.
A1 Faísca, Patrícia F.N.
A1 Rey Gayo, Antonio
AB We perform extensive lattice Monte Carlo simulations of protein folding to construct and compare the equilibrium and the kinetic transition state ensembles of a model protein that folds to the native state with two-state kinetics. The kinetic definition of the transition state is based on the folding probability analysis method, and therefore on the selection of conformations with 0.4<Pfold<0.6, while for the equilibrium characterization we consider conformations for which the evaluated values of several reaction coordinates correspond to the maximum of the free energy measured as a function of those reaction coordinates. Our results reveal a high degree of structural similarity between the ensembles determined by the two methods. However, the folding probability distribution of the conformations belonging to our definition of the equilibrium transition state (0.2<Pfold<0.8) is broader than that displayed by the kinetic transition state.
PB American Institute of Physics
SN 0021-9606
YR 2010
FD 2010
LK https://hdl.handle.net/20.500.14352/42702
UL https://hdl.handle.net/20.500.14352/42702
LA eng
NO Ministerio de Ciencia e Innovación (MICINN)
NO Conselho de Reitores das Universidades Portuguesas
DS Docta Complutense
RD 7 abr 2025