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.This work was supported by the Wellcome Trust (WT 095195MA). M.D.C. is supported by a BBSRC studentship; L.D...
Many intrinsically disordered proteins (IDPs) attain a well-defined structure in a coupled folding a...
In this work, we quantitatively investigate the thermodynamic analogy between the folding of monomer...
Intrinsically disordered proteins and regions (IDPs/Rs) are proteins that do not form stable and wel...
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of proteins are...
Intrinsically disordered proteins (IDPs) are recognized to play important roles in many biological f...
Protein or protein regions that are not forming well-defined structures in their free states under ...
International audienceIntrinsically Disordered Proteins (IDPs) are a class of protein that exert the...
In the past decade, a wealth of experimental data has demonstrated that a large fraction of proteins...
Intrinsically disordered proteins (IDPs) can be generally described as a class of proteins that lack...
International audienceIntrinsically disordered proteins (IDPs) are strongly represented in functiona...
Intrinsically disordered proteins (IDPs) widely participate in molecular recognition and signaling p...
ABSTRACT: Coupled folding and binding of intrinsically disordered proteins (IDPs) is prevalent in bi...
In the past decade, a wealth of experimental data has demonstrated that a large fraction of proteins...
Many intrinsically disordered proteins (IDPs) adopt a well-defined structure upon binding to their i...
Intrinsically disordered proteins represent a large class of proteins that lack a well-defined three...
Many intrinsically disordered proteins (IDPs) attain a well-defined structure in a coupled folding a...
In this work, we quantitatively investigate the thermodynamic analogy between the folding of monomer...
Intrinsically disordered proteins and regions (IDPs/Rs) are proteins that do not form stable and wel...
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of proteins are...
Intrinsically disordered proteins (IDPs) are recognized to play important roles in many biological f...
Protein or protein regions that are not forming well-defined structures in their free states under ...
International audienceIntrinsically Disordered Proteins (IDPs) are a class of protein that exert the...
In the past decade, a wealth of experimental data has demonstrated that a large fraction of proteins...
Intrinsically disordered proteins (IDPs) can be generally described as a class of proteins that lack...
International audienceIntrinsically disordered proteins (IDPs) are strongly represented in functiona...
Intrinsically disordered proteins (IDPs) widely participate in molecular recognition and signaling p...
ABSTRACT: Coupled folding and binding of intrinsically disordered proteins (IDPs) is prevalent in bi...
In the past decade, a wealth of experimental data has demonstrated that a large fraction of proteins...
Many intrinsically disordered proteins (IDPs) adopt a well-defined structure upon binding to their i...
Intrinsically disordered proteins represent a large class of proteins that lack a well-defined three...
Many intrinsically disordered proteins (IDPs) attain a well-defined structure in a coupled folding a...
In this work, we quantitatively investigate the thermodynamic analogy between the folding of monomer...
Intrinsically disordered proteins and regions (IDPs/Rs) are proteins that do not form stable and wel...