Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins.

ABSTRACT: The energy landscape theory provides a general framework for describing protein folding reactions. Because a large number of studies, however, have focused on two-state proteins with single well-defined folding pathways and without detectable intermediates, the extent to which free energy landscapes are shaped up by the native topology at the early stages of the folding process has not been fully characterized experimentally. To this end, we have investigated the folding mechanisms of two homologous three-state proteins, PTP-BL PDZ2 and PSD-95 PDZ3, and compared the early and late transition states on their folding pathways. Through a combination of Phi value analysis and molecular dynamics simulations we obtained atomic-level structures of the transition states of these homologous three-s

SUBMITTER: Calosci N 

PROVIDER: S-EPMC2614746 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature