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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.

Chromatin Immunoprecipitation- ChIP

Chromatin Immunoprecipitation- ChIP

Chromatin immunoprecipitation, or ChIP, is an antibody-based technique used to identify sites on DNA that bind to transcription factors of interest or histone proteins. It also helps determine the type of histone modifications such as acetylation, phosphorylation, or methylation.
Types of ChIP
ChIP can be divided into two types - X-ChIP and N-ChIP. X-ChIP involves in vivo cross-linking of histones and regulatory proteins to DNA, fragmenting the DNA by sonication, and isolating the protein-DNA...

Two-Dimensional (2D) NMR: Overview

Two-Dimensional (2D) NMR: Overview

The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse....

Chromatin Packaging

Chromatin Packaging

Each human somatic cell contains 6 billion base-pairs of DNA. Each base-pair is 0.34 nm long, which means that each diploid cell contains a staggering 2 meters of DNA. How is such a long DNA strand packed inside a nucleus measuring only 10 - 20 microns in diameter?
The chromatin
In combination with specialized DNA binding protein called Histones, the DNA double helix forms a compact DNA: protein complex called chromatin. The chromatin itself is further compacted into higher-order...

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Related Experiment Video

Updated: Jun 12, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Structural and dynamic studies of chromatin by solid-state NMR spectroscopy.

Christopher P Jaroniec¹

¹Department of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, Ohio 43210, USA.

Current Opinion in Structural Biology

|September 18, 2024

Summary

Magic angle spinning solid-state NMR provides atomistic insights into chromatin structure and dynamics. This technique characterizes histone domains in nucleosomes, revealing functional and mechanistic details of genome regulation.

Keywords:

Dynamic nuclear polarization Gene regulation Histone MAS solid-state NMR Nucleosome

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Area of Science:

Structural biology
Molecular biology
Biophysics

Background:

Chromatin, a complex of DNA and histone proteins, regulates genome accessibility and gene expression through dynamic state changes.
Histone post-translational modifications and interactions with chromatin modulators influence chromatin's open and compact states.
Advanced structural biology techniques like X-ray crystallography, cryo-electron microscopy, and NMR spectroscopy have enabled chromatin studies.

Purpose of the Study:

To highlight recent applications of magic angle spinning solid-state NMR for chromatin characterization.
To provide atomistic insights into the structure, conformational dynamics, and interactions of histone domains within condensed chromatin.
To mimic cellular chromatin densities in nucleosome and oligonucleosome arrays for realistic environmental studies.

Main Methods:

Utilized magic angle spinning solid-state NMR spectroscopy, an emerging technique for biomacromolecular assemblies.
Focused on characterizing histone core and tail domains within nucleosomes and oligonucleosome arrays.
Applied the technique to condensed chromatin mimicking high cellular densities.

Main Results:

Demonstrated the capability of magic angle spinning solid-state NMR to provide atomistic information for both rigid and flexible regions of chromatin.
Enabled detailed characterization of structure, conformational dynamics, and interactions of histone domains.
Provided insights into chromatin organization at high densities relevant to the cellular environment.

Conclusions:

Magic angle spinning solid-state NMR is a powerful technique for elucidating chromatin structure and dynamics at an atomic level.
The findings offer crucial functional and mechanistic insights into how chromatin regulates genome accessibility and gene expression.
This approach advances our understanding of chromatin organization and function in a cellular context.