Abstract
We have used optical tweezers to revisit the energy landscape of E. coli RNase H under mechanical force. This protein's equilibrium energetics and folding pathway have been studied in bulk and in single-molecule mechanical denaturation experiments, which showed the presence of a collapsed folding intermediate that is on-pathway to the native state (1). Taking advantage of improvements in our optical tweezers instrumentation, we have now revealed the existence of a short-lived high-energy unfolding intermediate. Our data suggest that this intermediate is obligatory in the mechanical unfolding pathway for this protein. This unfolding intermediate appears to be a local, partial denaturation of the C-terminus of the protein's structure. We explore the energetics of this transient state, and characterize how it defines the unfolding kinetics of RNase H. 1) Cecconi, Shank, Bustamante, Marqusee. Science 2005
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