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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...
Redox Reactions01:24

Redox Reactions

Oxidation-reduction or redox reactions involve the transfer of electrons from one molecule or atom to another. When an atom gains an electron, another atom must lose an electron, meaning oxidation and reduction must occur together. Since the redox occurs in pairs, the atom that gets oxidized is also called the reducing agent or reductant, and the atom that is reduced is also called the oxidizing agent or oxidant. A straightforward way to remember the definitions of oxidation and reduction is...
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...

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Related Experiment Video

Updated: Jun 21, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Rubredoxin as a paramagnetic relaxation-inducing probe.

Rui M Almeida1, Sofia R Pauleta, Isabel Moura

  • 1REQUIMTE/CQFB, Departamento de Química, Universidade Nova de Lisboa, Caparica, Portugal.

Journal of Inorganic Biochemistry
|August 5, 2009
PubMed
Summary
This summary is machine-generated.

Researchers utilized paramagnetic effects from metal centers to map protein interfaces in electron transfer complexes. This novel approach successfully identified binding sites in a cytochrome c(3) and rubredoxin complex using NMR spectroscopy.

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Area of Science:

  • Biochemistry and Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • Paramagnetic effects from metal centers were historically viewed as limitations in protein Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Recent advancements allow leveraging these paramagnetic effects as a tool for structural and functional studies of protein complexes.

Purpose of the Study:

  • To employ the paramagnetic effect of a metal center to map the interface of an electron transfer complex.
  • To investigate the binding interactions between Desulfovibrio gigas cytochrome c(3) and Fe-rubredoxin using NMR spectroscopy.

Main Methods:

  • Utilized a paramagnetic probe (Fe-rubredoxin) to induce specific line broadening in heme IV methyl resonances of cytochrome c(3).
  • Performed heteronuclear 2D NMR titration to identify the rubredoxin binding surface on cytochrome c(3).
  • Combined NMR data with restrained molecular docking simulations to predict complex structures.

Main Results:

  • Specific line broadening was observed in heme IV methyl resonances (M2(1) and M18(1)) of cytochrome c(3) upon interaction with rubredoxin.
  • NMR titration identified specific heme methyls on cytochrome c(3) as being involved in the binding interface.
  • Molecular docking simulations corroborated the NMR findings, showing a cluster of predicted binding solutions near heme IV.

Conclusions:

  • The study demonstrates the successful application of paramagnetic effects for mapping protein-protein interaction interfaces in electron transfer complexes.
  • The combination of paramagnetic NMR titration and molecular simulations provides a powerful strategy for studying complexes involving non-heme iron proteins and cytochromes.
  • This approach overcomes previous limitations of paramagnetic effects, turning a hindrance into a valuable analytical tool.