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Applications Of NMR In Biology

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Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
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Related Experiment Video

Updated: May 7, 2026

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode

Published on: June 4, 2021

Screening protein--single stranded RNA complexes by NMR spectroscopy for structure determination.

Jaelle N Foot¹, Mikael Feracci¹, Cyril Dominguez¹

¹Department of Biochemistry, Henry Wellcome Laboratories of Structural Biology, University of Leicester, UK.

Methods (San Diego, Calif.)

|October 8, 2013

Summary

RNA binding proteins (RBPs) regulate biological processes and are implicated in diseases like cancer. Understanding their RNA targets is key for drug discovery, and Nuclear Magnetic Resonance (NMR) is a powerful tool for studying these complexes.

Keywords:

NMR spectroscopy Protein–RNA complex STAR proteins Sam68 T-STAR

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Area of Science:

Molecular Biology
Biochemistry
Structural Biology

Background:

RNA molecules have emerged as critical regulators in biological processes, moving beyond their traditional role in genetic information transfer.
The identification of numerous RNA binding proteins (RBPs) and the link between mutations in RNA or RBPs and diseases like cancer highlight their significance.
Understanding the specific molecular interactions between proteins and RNA is essential for developing targeted therapies for diseases involving protein-RNA complexes.

Purpose of the Study:

To describe a Nuclear Magnetic Resonance (NMR) strategy for optimizing conditions for structural studies of protein-single stranded RNA complexes.
To provide a framework for investigating the molecular basis of protein-RNA recognition.
To facilitate drug discovery efforts targeting protein-RNA interactions.

Main Methods:

Utilizing Nuclear Magnetic Resonance (NMR) spectroscopy as a primary technique for atomic-level structural analysis.
Developing and screening optimal experimental conditions for studying protein-RNA complexes.
Employing specific proteins, Sam68 and T-STAR, as model systems for method development.

Main Results:

Established a robust NMR strategy for screening conditions for structural studies of protein-single stranded RNA complexes.
Demonstrated the applicability of the NMR approach using Sam68 and T-STAR proteins.
Provided a foundation for future structural investigations of various protein-RNA interactions.

Conclusions:

Nuclear Magnetic Resonance (NMR) is a highly effective technique for elucidating the structure of protein-RNA complexes at the atomic level.
The described NMR strategy aids in identifying optimal conditions for structural studies, crucial for drug discovery.
Further research into protein-RNA complexes using NMR can lead to novel therapeutic interventions for RNA-related diseases.