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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...
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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Translational Diffusion and Self-Association of an Intrinsically Disordered Protein κ-Casein Using NMR with

Daria L Melnikova1, Venkatesh V Ranjan2,3, Yuri E Nesmelov3

  • 1Department of Physics of Molecular Systems, Kazan Federal University, Kazan 420011, Russia.

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Intrinsically disordered proteins (IDPs) like κ-casein show continuous self-association, leading to phase separation or gel formation depending on concentration. This behavior is more dynamic than α-casein.

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Area of Science:

  • Biophysics
  • Protein Chemistry

Background:

  • Translational diffusion of globular proteins is well-studied.
  • Translational diffusion of intrinsically disordered proteins (IDPs) remains less understood.

Purpose of the Study:

  • Investigate the translational diffusion of the IDP κ-casein.
  • Determine how κ-casein self-association impacts its diffusion and structural behavior.

Main Methods:

  • Pulsed-field gradient nuclear magnetic resonance (PFG-NMR).
  • Time-resolved Förster resonance energy transfer (TR-FRET).

Main Results:

  • κ-casein exhibits continuous self-association.
  • Below 0.08 volume fraction, self-association causes phase separation at 4 °C.
  • Above 0.08 volume fraction, labile gel-like networks form without phase separation.
  • Compared to α-casein, κ-casein forms less extensive and more dynamic networks.

Conclusions:

  • κ-casein's self-association properties are unique.
  • Findings enhance understanding of κ-casein behavior and its role in casein micelle formation.