IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding.

ABSTRACT: The structural states of proteins include ordered globular domains as well as intrinsically disordered protein regions that exist as highly flexible conformational ensembles in isolation. Various computational tools have been developed to discriminate ordered and disordered segments based on the amino acid sequence. However, properties of IDRs can also depend on various conditions, including binding to globular protein partners or environmental factors, such as redox potential. These cases provide further challenges for the computational characterization of disordered segments. In this work we present IUPred2A, a combined web interface that allows to generate energy estimation based predictions for ordered and disordered residues by IUPred2 and for disordered binding regions by ANCHOR2. Th

SUBMITTER: Meszaros B 

PROVIDER: S-EPMC6030935 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature