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Related Concept Videos

Applications Of NMR In Biology01:25

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.
The...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
Nuclear Magnetic Resonance (NMR): Overview01:07

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...
Two-Dimensional (2D) NMR: Overview01:12

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.
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

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Related Experiment Video

Updated: Jun 30, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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

Published on: September 17, 2017

Structural biology by NMR: structure, dynamics, and interactions.

Phineus R L Markwick1, Thérèse Malliavin, Michael Nilges

  • 1Département de Biologie Structurale et Chimie, Institut Pasteur, Unité de Bio-Informatique Structurale, CNRS URA 2185, Paris, France.

Plos Computational Biology
|September 27, 2008
PubMed
Summary

Nuclear Magnetic Resonance (NMR) spectroscopy reveals bio-macromolecule structure and dynamics. Molecular dynamics simulations are crucial for interpreting complex NMR data to understand molecular function.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Bio-macromolecule function relies on 3D structure and dynamic conformational changes.
  • These molecules exhibit inherent flexibility across a wide range of timescales (picoseconds to seconds).
  • Understanding these dynamics is key to comprehending biological processes.

Purpose of the Study:

  • To highlight the role of Nuclear Magnetic Resonance (NMR) spectroscopy in studying protein structure and dynamics.
  • To address the challenge of integrating structural and dynamic information from NMR data.
  • To emphasize the utility of molecular dynamics simulations in analyzing NMR experimental results.

Main Methods:

  • Utilizing Nuclear Magnetic Resonance (NMR) spectroscopy for probing bio-macromolecular structure and dynamics in solution.
  • Employing advanced experimental techniques and computational methodologies.
  • Leveraging molecular dynamics simulations to interpret complex NMR data.

Main Results:

  • NMR experiments provide data sensitive to both structural features and molecular dynamics.
  • A consistent interpretation of structure and dynamics from NMR data remains a significant challenge.
  • Molecular dynamics simulations have proven indispensable for analyzing NMR data.

Conclusions:

  • Integrating structural and dynamic information from NMR is crucial for understanding bio-macromolecule function.
  • Molecular dynamics simulations are essential tools for overcoming challenges in NMR data analysis.
  • Further advancements in computational methods will enhance the interpretation of NMR data for biological insights.