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Applications Of NMR In Biology

Applications Of NMR In Biology

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.

Nuclear Magnetic Resonance (NMR): Overview

Nuclear Magnetic Resonance (NMR): Overview

Nuclear magnetic resonance (NMR) is a phenomenon exhibited by certain nuclei that can absorb characteristic radio frequency radiation under certain conditions. NMR has been extensively applied in molecular spectroscopy and medical diagnostic imaging. In both these applications, the molecule or subject under study is placed in a magnetic field and irradiated with radio frequency energy.
NMR spectroscopy generates a spectrum where the characteristic absorption frequencies of the sample are...

Viral Structure

Viral Structure

Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.

Atomic Nuclei: Magnetic Resonance

Atomic Nuclei: Magnetic Resonance

The number of nuclear spins aligned in the lower energy state is slightly greater than those in the higher energy state. In the presence of an external magnetic field, as the spins precess at the Larmor frequency, the excess population results in a net magnetization oriented along the z axis. When a pulse or a short burst of radio waves at the Larmor frequency is applied along the x axis, the coupling of frequencies causes resonance and flips the nuclear spins of the excess population from the...

Cryo-electron Microscopy

Cryo-electron Microscopy

Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...

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Related Experiment Video

Updated: May 7, 2025

Open-source Single-particle Analysis for Super-resolution Microscopy with VirusMapper

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Published on: April 9, 2017

Nuclear Magnetic Resonance Spectroscopy to Study Virus Structure.

José L Neira^1,2

¹IDIBE, Universidad Miguel Hernández, Elche, Alicante, Spain. jlneira@umh.es.

Sub-Cellular Biochemistry

|December 31, 2024

Summary

This summary is machine-generated.

Nuclear magnetic resonance (NMR) spectroscopy reveals viral protein structures and dynamics. This technique is crucial for understanding viral protein interactions, conformational changes, and disordered proteins, aiding in virus life cycle studies.

Keywords:

Assembly Binding Capsid Chemical shifts Conformational changes Coupling constants Dynamics Electron paramagnetic resonance (EPR)Equilibrium Flexibility Hydrogen exchange Lipids Membrane Nuclear magnetic resonance (NMR)Nucleic acid Protein-nucleic acid interactions Protein-protein interactions Solid-state Solution structure Unfolded protein Virus

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Area of Science:

Biophysics
Structural Biology
Virology

Background:

Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for analyzing molecular structures and dynamics.
It has been widely applied in virology to study viral proteins, nucleic acids, and their interactions.

Purpose of the Study:

To highlight the applications of NMR spectroscopy in virology.
To demonstrate NMR's capability in elucidating viral protein structures, dynamics, and interactions.

Main Methods:

Utilizing Nuclear Magnetic Resonance (NMR) spectroscopy in both liquid and solid-state.
Complementing NMR with X-ray crystallography and electron microscopy for structural studies.

Main Results:

NMR enables the "bottom-up" structural determination of viral protein domains and their interactions.
It reveals conformational changes and dynamic equilibria in viral proteins and nucleic acids.
NMR provides atomic-level insights into intrinsically disordered viral proteins and thermodynamic binding parameters.

Conclusions:

NMR spectroscopy is instrumental in understanding viral protein structure, dynamics, and function.
Its integration with other techniques enhances the study of complex viral systems.
NMR is essential for characterizing viral components and their behavior during infection and assembly.