Generating NMR chemical shift assignments of intrinsically disordered proteins using carbon-detected NMR methods.

ABSTRACT: There is an extraordinary need to describe the structures of intrinsically disordered proteins (IDPs) due to their role in various biological processes involved in signaling and transcription. However, general study of IDPs by NMR spectroscopy is limited by the poor (1)H amide chemical shift dispersion typically observed in their spectra. Recently, (13)C direct-detected NMR spectroscopy has been recognized as enabling broad structural study of IDPs. Most notably, multidimensional experiments based on the (15)N,(13)C CON spectrum make complete chemical shift assignment feasible. Here we document a collection of NMR-based tools that efficiently lead to chemical shift assignment of IDPs, motivated by a case study of the C-terminal disordered region from the human pancreatic transcription fact

SUBMITTER: Sahu D 

PROVIDER: S-EPMC3944900 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature