Mar 31, 2020

Criticality in the conformational phase transition among self-similar groups in intrinsically disordered proteins: probed by salt-bridge dynamics

BioRxiv : the Preprint Server for Biology
Guido GrimmAlastair John Potts


Intrinsically disordered proteins (IDP) serve as one of the key components in the proteome. In contrast to the dominant class of cytosolic globular proteins, they harbor an enormous amount of physical flexibility or structural plasticity enforcing them to be retained in conformational ensembles rather than well defined stable folds. Previous studies have revealed the importance of transient dynamical phenomena like that of salt-bridges within them to support their physical flexibility and have further suggested their functional importance. For their characteristic flexibility, these proteins remain amenable and accessible to different ordered binding partners, potentially supporting their multi-functionality. The current study addresses this complex structure-functional interplay in IDPs using phase transition dynamics to conceptualize the underlying mechanism of their being distributed across degenerate structural states (conformational ensembles). For this purpose, extensive molecular dynamics simulations have been done and the data analyzed from a statistical physics perspective. A major emphasis has been put on the plausible scope of self-organized criticality (SOC) to be implemented in the dynamics of the complex system of...Continue Reading

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