Related Experiment Video
Updated: Jun 29, 2026

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
Published on: November 2, 2018
Probing interactions by means of pulsed field gradient nuclear magnetic resonance spectroscopy
Sara Cozzolino1, Maria G Sanna, Massimiliano Valentini
1Agricultural Research Council, Research Centre for Plant Soil System, Instrumental Centre of Tor Mancina, S. P. Pascolarese-Strada della Neve Km 1, 00015 Monterotondo, Rome, Italy.
Abstract:
Molecular self-diffusion coefficients (D) of species in solution are related to size and shape and can be used for studying association phenomena. Pulsed field gradient nuclear magnetic resonance (PFG-NMR) spectroscopy has been revealed to be a powerful analytical tool for D measurement in different research fields. The present work briefly illustrates the use of PFG-NMR for assessing the existence of interactions in very different chemical systems: organic and organometallic compounds, colloidal materials and biological aggregates. The application of PFG-NMR is remarkable for understanding the role of anions in homogenous transition metal catalysis and for assessing the aggregation behaviour of biopolymers in material science.
Related Concept Videos
Insensitive Nuclei Enhanced by Polarization Transfer (INEPT)
Double Resonance Techniques: Overview
Spin decoupling is usually achieved by...
NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences
Applications Of NMR In Biology
The...
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...
NMR Spectroscopy: Spin–Spin Coupling

