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Related Concept Videos

Paramagnetism01:30

Paramagnetism

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Paramagnets are materials with unpaired electrons that possess a finite magnetic moment. In the absence of a magnetic field, these moments are randomly oriented, and thus the net moment is zero. Under an external field, a torque acting on the moments tends to align them along the field's direction. However, the random thermal motion of electrons produces a torque opposite to the external field and tries to disorient the moments. These two competing effects align only a few moments along the...
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Atomic Nuclei: Nuclear Relaxation Processes01:23

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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.
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Related Experiment Video

Updated: Sep 3, 2025

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Approaching Protein Aggregation and Structural Dynamics by Equilibrium and Nonequilibrium Paramagnetic Perturbation.

Yamanappa Hunashal1,2, Mathias Percipalle1,3, Tamás Molnár4

  • 1Chemistry Program, Science Division, New York University Abu Dhabi, Abu Dhabi 129188, United Arab Emirates.

Analytical Chemistry
|July 25, 2022
PubMed
Summary

PENELOP, a novel nuclear magnetic resonance (NMR) method, maps protein surface accessibility and dynamics. This sensitive technique aids in studying protein interactions and conformational changes at physiological concentrations.

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Area of Science:

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

Background:

  • Understanding protein structure-function relationships requires characterizing surface accessibility, dynamics, and interactions.
  • Existing NMR techniques for these analyses can be demanding and require high sample concentrations.

Purpose of the Study:

  • To introduce PENELOP (Paramagnetic Equilibrium vs Nonequilibrium magnetization Enhancement or LOss Perturbation), a novel NMR approach.
  • To demonstrate PENELOP's capability in simultaneously assessing protein surface exposure, hindered accessibility, and μs-ms timescale exchange processes.
  • To provide a sensitive alternative for studying protein dynamics and interactions at low, physiologically relevant concentrations.

Main Methods:

  • Application of the PENELOP NMR technique.
  • Analysis of paramagnetic equilibrium and nonequilibrium magnetization perturbations.
  • Distinguishing conformational mobility from chemical exchange processes.

Main Results:

  • PENELOP successfully maps protein surface accessibility.
  • The method differentiates conformational mobility from chemical exchange.
  • High sensitivity allows studies at low, physiologically relevant protein concentrations.
  • PENELOP was applied to a SARS-CoV-2 replication-transcription complex component and an amyloidogenic protein, addressing association, dynamics, and oligomerization.

Conclusions:

  • PENELOP offers a versatile and sensitive NMR method for comprehensive protein characterization.
  • It provides an alternative to more demanding techniques for studying protein dynamics and interactions.
  • The approach is valuable for investigating complex biological systems, including viral components and disease-related proteins.