Abstract
Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure. Since their identification more than a decade ago, many questions regarding their functional relevance and interaction mechanisms remain unanswered. Although most experiments have taken equilibrium and structural perspectives, fewer studies have investigated the kinetics of their interactions. Here we review and highlight the type of information that can be gained from kinetic studies. In particular, we show how kinetic studies of coupled folding and binding reactions, an important class of signaling event, are needed to determine mechanisms.
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CITATION STYLE
Shammas, S. L., Crabtree, M. D., Dahal, L., Wicky, B. I. M., & Clarke, J. (2016, March 25). Insights into coupled folding and binding mechanisms from kinetic studies. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology Inc. https://doi.org/10.1074/jbc.R115.692715
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