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Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies
Authors:Sarah L. Shammas  Michael D. Crabtree  Liza Dahal  Basile I. M. Wicky  Jane Clarke
Affiliation:From the Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
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.
Keywords:biophysics   electrostatics   kinetics   protein dynamic   protein folding   signaling   coupled folding and binding   phi-value   protein-protein interactions   residual structure   IDP   protein electrostatics
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