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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Dynamical Buffering of Reconfiguration Dynamics in Intrinsically Disordered Proteins.

Miloš T Ivanović1, Andrea Holla1, Mark F Nüesch1

  • 1Department of Biochemistry, University of Zurich, Zurich 8057, Switzerland.

JACS Au
|March 27, 2026
PubMed
Summary

Intrinsically disordered protein dynamics are crucial for function. Despite sequence variations, chain reconfiguration times remain surprisingly constant due to competing factors, buffering sequence effects on linker dynamics.

Keywords:
all-atom molecular dynamicschain reconfiguration timenanosecond fluorescence correlation spectroscopysalt bridgessingle-molecule FRETsingle-molecule spectroscopy

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Area of Science:

  • Biophysics
  • Protein Dynamics
  • Molecular Biology

Background:

  • Intrinsically disordered proteins (IDPs) possess dynamic conformational ensembles essential for their function.
  • The relationship between the amino acid sequence of IDPs and their chain dynamics is not well understood.
  • Understanding IDP dynamics is key to deciphering their roles in cellular processes.

Purpose of the Study:

  • To investigate how sequence composition affects the dynamics of intrinsically disordered protein regions.
  • To explore the relationship between chain dimensions and reconfiguration times in diverse IDP sequences.
  • To elucidate the molecular mechanisms underlying the observed dynamics.

Main Methods:

  • Single-molecule Förster Resonance Energy Transfer (smFRET) to infer chain dimensions.
  • Nanosecond Fluorescence Correlation Spectroscopy (nsFCS) to measure chain reconfiguration times.
  • Multimicrosecond all-atom explicit-solvent molecular dynamics (MD) simulations.

Main Results:

  • Chain dimensions varied significantly with sequence, as inferred from smFRET.
  • Chain reconfiguration times measured by nsFCS showed minimal dependence on sequence composition.
  • MD simulations accurately reproduced experimental FRET efficiencies and confirmed the lack of correlation between reconfiguration times and chain dimensions.

Conclusions:

  • Compensating dynamic factors, namely narrowing end-to-end distance distributions and reduced intrachain diffusion, buffer the effect of sequence on linker dynamics.
  • This buffering mechanism may allow for functional conservation across evolving IDP sequences.
  • The study provides a molecular-level explanation for the sequence-independent dynamics observed in certain disordered protein regions.