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Default Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.

Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.

Related Articles Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.

Anal Biochem. 2013 Dec 9;

Authors: Sahu D, Bastidas M, Showalter S

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, multi-dimensional 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 factor Pdx1. Our strategy builds on the combination of two 3D experiments, (HN-flip)N(CA)CON and 3D (HN-flip)N(CA)NCO, that enable daisy-chain connections to be built along the IDP backbone, facilitated by acquisition of amino-acid specific (15)N,(13)C-CON detected experiments. Assignments are completed through carbon-detected, TOCSY based side chain chemical shift measurement. Conducting our study required producing valuable modifications to many previously published pulse sequences, motivating us to announce the creation of a database of our pulse programs, which we make freely available through the web.


PMID: 24333248 [PubMed - as supplied by publisher]



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