Related Experiment Video
Updated: May 13, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Estimating side-chain order in [U-2H;13CH3]-labeled high molecular weight proteins from analysis of HMQC/HSQC spectra
Vitali Tugarinov1, Lewis E Kay
1Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA. vitali@umd.edu
Abstract:
A simple approach for quantification of methyl-containing side-chain mobility in high molecular weight methyl-protonated, uniformly deuterated proteins is described, based on the measurement of peak intensities in methyl (1)H-(13)C HMQC and HSQC correlation maps and relaxation rates of slowly decaying components of methyl (1)H-(13)C multiple-quantum coherences. A strength of the method is that [U-(2)H;(13)CH3]-labeled protein samples are required that are typically available at an early stage of any analysis. The utility of the methodology is demonstrated with applications to three protein systems ranging in molecular weight from 82 to 670 kDa. Although the approach is only semiquantitative, a high correlation between order parameters extracted via this scheme and other more established methods is nevertheless demonstrated.
More Related Videos
Related Concept Videos
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)
High-Resolution Mass Spectrometry (HRMS)
¹H NMR: Interpreting Distorted and Overlapping Signals
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
2D NMR: Overview of Heteronuclear Correlation Techniques
NMR Spectroscopy Of Amines

