Contrasting the individual reactive pathways in protein unfolding and disulfide bond reduction observed within a single protein.

ABSTRACT: Identifying the dynamics of individual molecules along their reactive pathways remains a major goal of modern chemistry. For simple chemical reactions, the transition state position is thought to be highly localized. Conversely, in the case of more complex reactions involving proteins, the potential energy surfaces become rougher, resulting in heterogeneous reaction pathways with multiple transition state structures. Force-clamp spectroscopy experimentally probes the individual reaction pathways sampled by a single protein under the effect of a constant stretching force. Herein, we examine the distribution of conformations that populate the transition state of two different reactions; the unfolding of a single protein and the reduction of a single disulfide bond, both occurring within the

SUBMITTER: Garcia-Manyes S 

PROVIDER: S-EPMC3070170 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature