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Updated: Jul 1, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
An NMR experiment for simultaneous TROSY-based detection of amide and methyl groups in large proteins
Chenyun Guo1, Daoning Zhang, Vitali Tugarinov
1Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA.
Abstract:
A sensitive 2D NMR experiment for simultaneous time-shared TROSY-type detection of amide and methyl groups in high-molecular-weight proteins is described. The pulse scheme is designed to preserve the slowly decaying components of both 1H-15N and methyl 13CH3 spin systems in the course of indirect evolution and acquisition periods. The proposed methodology is applied to the study of substrate binding to {U-[15N,2H]; Ile-[13CH3]; Leu,Val-[13CH3/12CD3]}-labeled 82-kDa enzyme Malate Synthase G and is expected to accelerate NMR-based screening of large proteins labeled with 15N and selectively labeled with 13CH3 at methyl sites.
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