Related Experiment Video
Updated: May 10, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
High-dimensional NMR spectra for structural studies of biomolecules
Krzysztof Kazimierczuk1, Jan Stanek, Anna Zawadzka-Kazimierczuk
1Centre of New Technologies, University of Warsaw, Żwirki i Wigury 93, 02-089 Warsaw (Poland).
Abstract:
Recent developments in the acquisition and processing of NMR data sets facilitate the recording of ultra-high-resolution NMR spectra in a reasonable time. The new experiments allow easy resonance assignment for folded and unfolded proteins, as well as the precise determination of spectral parameters, for example, chemical shifts, NOE contacts, coupling constants or cross-correlated relaxation rates. Owing to exceptional resolution of 4D-6D spectroscopy, detailed studies of biomolecules of unprecedented complexity are now possible. Herein, the principles of acquisition and processing methods are presented. The main applications of high-dimensional NMR experiments, including backbone and side-chain resonance assignment in proteins, as well as heteronuclear edited NOE techniques are reviewed.
Related Concept Videos
Two-Dimensional (2D) NMR: Overview
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse.
2D NMR: Overview of Heteronuclear Correlation Techniques
2D NMR: Overview of Homonuclear Correlation Techniques
COSY90 is the standard two-dimensional (2D) COSY experiment that...
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)
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...
Applications Of NMR In Biology
The...
