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Updated: Jun 18, 2026
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Protocol for expressing and purifying recombinant full-length Tau by combining affinity chromatography with
Ruiheng Jing1, Sayanta Mahapatra1, Abhishek Bimali1
1University of Colorado, Department of Chemistry, Boulder, CO 80309, USA.
Abstract:
Deposits of microtubule-associated protein full-length Tau (Tau2N4R) are implicated as a hallmark of Alzheimer's disease. Its biochemical and structural characterization is key to understanding disease progression, aggregate toxicity, and designing therapeutics. We present a protocol for expressing and purifying Tau2N4R by combining affinity chromatography with preparative high-performance liquid chromatography (HPLC). We describe steps for linking an N-terminal hexahistidine tag and a cleavable SUMO tag to Tau2N4R. This purification ensures an ultrapure Tau2N4R that gives rise to heparin-induced and cofactor-free in vitro fibrillation.
