Molecular origin of the differential stabilities of the protofilaments in different polymorphs: molecular dynamics simulation and deep learning.

Fragments of α-synuclein, an intrinsically disordered protein, whose misfolding and aggregation are responsible for diseases like Parkinson's disease and others, can co-exist in different polymorphs like 'rod' and 'twister'. Their apparently stable structures have different degrees of tolerance to perturbations like point mutations. The molecular basis of this is investigated using molecular dynamics-based conformational sampling.

Remote communication between unstructured and structured regions of Bcl-2 tunes its ligand binding capacity: Mechanistic insights.

Bcl-2, the prototypic, anti-apoptotic member of Bcl-2 family possesses a long Intrinsically Disordered Region (IDR) of more than sixty amino acid residues. In spite of a number of experimental evidences on the influence of IDR to regulate the function of the protein, the molecular basis is not yet established. The present work with ~8µs conformational sampling of Bcl-2, using molecular dynamics in all atom description, offers a molecular mechanistic insight into the communication between the IDR and the structured region.