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Related Concept Videos

Atomic Nuclei: Types of Nuclear Relaxation01:28

Atomic Nuclei: Types of Nuclear Relaxation

Nuclear relaxation restores the equilibrium population imbalance and can occur via spin–lattice or spin–spin mechanisms, which are first-order exponential decay processes.
In spin–lattice or longitudinal relaxation, the excited spins exchange energy with the surrounding lattice as they return to the lower energy level. Among several mechanisms that contribute to spin–lattice relaxation, magnetic dipolar interactions are significant. Here, the excited nucleus transfers energy to a nearby...
Atomic Nuclei: Nuclear Relaxation Processes01:23

Atomic Nuclei: Nuclear Relaxation Processes

In the absence of an external magnetic field, nuclear spin states are degenerate and randomly oriented. When a magnetic field is applied, the spins begin to precess and orient themselves along (lower energy) or against (higher energy) the direction of the field. At equilibrium, a slight excess population of spins exists in the lower energy state. Because the direction of the magnetic field is fixed as the z-axis,  the precessing magnetic moments are randomly oriented around the z-axis. This...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...

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Related Experiment Video

Updated: May 17, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Isotope labeling methods for relaxation measurements.

Patrik Lundström1, Alexandra Ahlner, Annica Theresia Blissing

  • 1Department of Physics, Chemistry and Biology, Linköping University, Linköping, Sweden. patlu@ifm.liu.se

Advances in Experimental Medicine and Biology
|October 19, 2012
PubMed
Summary
This summary is machine-generated.

Nuclear magnetic spin relaxation is a key method for studying molecular dynamics. This chapter discusses selective isotopic labeling strategies to improve protein dynamics measurements using nuclear magnetic resonance (NMR).

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15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
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Last Updated: May 17, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Area of Science:

  • Biophysics
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Nuclear magnetic spin relaxation is a powerful tool for analyzing molecular dynamics, including reorientation and internal motions.
  • Traditional methods using uniformly (15)N labeled samples have limitations in sensitivity and scope for complex systems.
  • Probing dynamics at specific sites like methyl groups or using (13)C or (1)H nuclei enhances sensitivity and structural characterization, especially for large molecules or low-populated states.

Purpose of the Study:

  • To explore the application of nuclear magnetic spin relaxation for detailed molecular dynamics analysis.
  • To highlight the limitations of uniform isotopic labeling in NMR studies of proteins.
  • To discuss the necessity and implementation of selective isotopic labeling schemes for advanced NMR experiments.

Main Methods:

  • Utilizing nuclear magnetic spin relaxation measurements to determine time constants for molecular reorientation.
  • Employing selective isotopic labeling strategies to target specific atomic positions within protein molecules.
  • Analyzing nuclear magnetic resonance (NMR) data to characterize internal motions across various timescales (picoseconds to seconds).

Main Results:

  • Demonstrated that selective labeling significantly enhances sensitivity for probing dynamics in large biomolecular systems.
  • Showcased how specific labeling enables structural characterization of low-populated protein states.
  • Identified potential artifacts from homonuclear scalar couplings in certain NMR experiments and proposed selective labeling as a solution.

Conclusions:

  • Selective isotopic labeling is crucial for overcoming limitations of uniform labeling in protein dynamics studies using NMR.
  • These advanced labeling techniques expand the applicability of nuclear magnetic spin relaxation for detailed molecular investigations.
  • The discussed schemes facilitate precise measurements of relaxation rates at numerous protein positions, advancing structural biology and biophysics.