Insights into the Binding of Intrinsically Disordered Proteins from Molecular Dynamics Simulation.

ABSTRACT: Intrinsically disordered proteins (IDPs) are a class of protein that, in the native state, possess no well-defined secondary or tertiary structure, existing instead as dynamic ensembles of conformations. They are biologically important, with approximately 20% of all eukaryotic proteins disordered, and found at the heart of many biochemical networks. To fulfil their biological roles, many IDPs need to bind to proteins and/or nucleic acids. And while unstructured in solution, IDPs typically fold into a well-defined three-dimensional structure upon interaction with a binding partner. The flexibility and structural diversity inherent to IDPs makes this coupled folding and binding difficult to study at atomic resolution by experiment alone, and computer simulation currently offers perhaps the b

SUBMITTER: Baker CM 

PROVIDER: S-EPMC8336759 | biostudies-literature | 2014 May-Jun

REPOSITORIES: biostudies-literature