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Related Concept Videos

Paramagnetism01:30

Paramagnetism

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...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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...
Diamagnetism01:26

Diamagnetism

Materials consisting of paired electrons have zero net magnetic moments. However, when these materials are placed under an external magnetic field, the moments opposite to the field are induced. Such materials are called diamagnets. Diamagnetism is the response of the diamagnets when placed in an external magnetic field.
Diamagnetism was discovered by Anton Brugmans in 1778 when he observed that bismuth gets repelled by magnetic fields, thus theorizing that diamagnets get repelled by magnets.
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved in...
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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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

Intermolecular dynamics studied by paramagnetic tagging.

Xingfu Xu1, Peter H J Keizers, Wolfgang Reinle

  • 1Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA, Leiden, The Netherlands.

Journal of Biomolecular NMR
|March 11, 2009
PubMed
Summary
This summary is machine-generated.

Yeast cytochrome c and bovine adrenodoxin form a dynamic protein complex. A novel lanthanide tag method reveals extensive surface sampling, crucial for understanding protein interactions.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Protein-protein interactions are fundamental to biological processes.
  • Electron transfer complexes, like yeast cytochrome c and bovine adrenodoxin, are vital in cellular respiration.
  • Understanding the dynamics of these complexes is key to elucidating their function.

Purpose of the Study:

  • To investigate the dynamic nature of the electron transfer complex formed by yeast cytochrome c and bovine adrenodoxin.
  • To demonstrate a novel method for probing protein complex dynamics using a lanthanide tag.
  • To quantify the interaction surface and dynamics of the complex.

Main Methods:

  • Utilized a rigid lanthanide tag (Caged Lanthanide NMR Probe 5) attached to yeast cytochrome c.
  • Employed Nuclear Magnetic Resonance (NMR) spectroscopy to measure pseudocontact shifts and residual dipolar couplings.
  • Performed computational simulations to analyze the observed NMR data and model protein dynamics.

Main Results:

  • The lanthanide tag successfully probed complex dynamics without perturbing the binding interface.
  • Observed very small residual dipolar couplings in adrenodoxin, indicating significant flexibility within the complex.
  • Simulations revealed that cytochrome c must sample a large portion of the adrenodoxin surface to explain the limited alignment.

Conclusions:

  • The yeast cytochrome c-bovine adrenodoxin complex is a dynamic encounter complex.
  • Lanthanide tagging provides a powerful, tag-based NMR approach to study protein complex dynamics and domain mobility.
  • This method offers a straightforward way to observe dynamics without requiring external alignment media.