Czechtizky W
How well does molecular simulation reproduce environment-specific conformations of the intrinsically disordered peptides PLP, TP2 and ONEG?
Intrinsically disordered proteins and peptides (IDPs) do not adopt stable secondary or tertiary structures, and are best structurally characterised as ensembles of flexible conformations.1 While the traditional paradigm holds that biological processes are mediated by macromolecules with fixed three-dimensional structures, it is now becoming increasingly evident that IDPs play a very important role.2 In the absence of a stable structure and characterised by high levels of flexibility, IDPs can easily interconvert between multiple conformations. This enables them to bind to different macromolecules, resulting in diverse functionality.2–6 For example, the intrinsically disordered N-terminal transactivation domain of the protein p53 is structured into a helix upon binding to a hydrophobic cleft in the proteins MDM2 or p300.3,7–9 Similarly the disordered C-terminal region of p53 has been shown to adopt diverse secondary structures when complexed to different protein partners.10 The study of the structural dynamics of IDPs and their participation in protein–protein interactions (PPIs) using computational and experimental studies is increasingly illuminating the subtle yet complex nature of molecular interactions governing biomolecular mechanisms.
ReadHow well does molecular simulation reproduce environment-specific conformations of the intrinsically disordered peptides PLP, TP2 and ONEG?
Intrinsically disordered proteins and peptides (IDPs) do not adopt stable secondary or tertiary structures, and are best structurally characterised as ensembles of flexible conformations.1 While the traditional paradigm holds that biological processes are mediated by macromolecules with fixed three-dimensional structures, it is now becoming increasingly evident that IDPs play a very important role.
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