Related Experiment Video
Updated: Dec 14, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions
Christopher A Waudby1, John Christodoulou2
1Institute of Structural and Molecular Biology, UCL and Birkbeck College, London, UK. c.waudby@ucl.ac.uk.
None:
Interactions of intrinsically disordered proteins are central to their cellular functions, and solution-state NMR spectroscopy provides a powerful tool for characterizing both structural and mechanistic aspects of such interactions. Here we focus on the analysis of IDP interactions using NMR titration measurements. Changes in resonance lineshapes in two-dimensional NMR spectra upon titration with a ligand contain rich information on structural changes in the protein and the thermodynamics and kinetics of the interaction, as well as on the microscopic association mechanism. Here we present protocols for the optimal design of titration experiments, data acquisition, and data analysis by two-dimensional lineshape fitting using the TITAN software package.
Related Concept Videos
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...
Intrinsically Disordered Proteins
Protein-protein Interfaces
Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

