Structure of a partially unfolded form of Escherichia coli dihydrofolate reductase provides insight into its folding pathway.

ABSTRACT: Proteins frequently fold via folding intermediates that correspond to local minima on the conformational energy landscape. Probing the structure of the partially unfolded forms in equilibrium under native conditions can provide insight into the properties of folding intermediates. To elucidate the structures of folding intermediates of Escherichia coli dihydrofolate reductase (DHFR), we investigated transient partial unfolding of DHFR under native conditions. We probed the structure of a high-energy conformation susceptible to proteolysis (cleavable form) using native-state proteolysis. The free energy for unfolding to the cleavable form is clearly less than that for global unfolding. The dependence of the free energy on urea concentration (m-value) also confirmed that the cleavable form i

SUBMITTER: Kasper JR 

PROVIDER: S-EPMC4253813 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature