DispHred: A Server to Predict pH-Dependent Order-Disorder Transitions in Intrinsically Disordered Proteins.

ABSTRACT: The natively unfolded nature of intrinsically disordered proteins (IDPs) relies on several physicochemical principles, of which the balance between a low sequence hydrophobicity and a high net charge appears to be critical. Under this premise, it is well-known that disordered proteins populate a defined region of the charge-hydropathy (C-H) space and that a linear boundary condition is sufficient to distinguish between folded and disordered proteins, an approach widely applied for the prediction of protein disorder. Nevertheless, it is evident that the C-H relation of a protein is not unalterable but can be modulated by factors extrinsic to its sequence. Here, we applied a C-H-based analysis to develop a computational approach that evaluates sequence disorder as a function of pH, assuming

SUBMITTER: Santos J 

PROVIDER: S-EPMC7461198 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature