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Related Experiment Video

Updated: May 23, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
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Published on: April 28, 2022

Kinetics and Spatial Distribution of β-Sheet Development in TDP-43CTD Condensate Maturation.

Sashary Ramos1, Matthew D Watson1, Jennifer C Lee1

  • 1Laboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, United States.

ACS Chemical Neuroscience
|May 22, 2026
PubMed
Summary
This summary is machine-generated.

Cytosolic inclusions of aggregated TAR DNA-binding protein 43 (TDP-43) are linked to neurodegenerative diseases. Raman spectroscopy revealed that TDP-43 condensates transition from disordered to beta-sheet structures over time, with water environment changes lagging behind.

Keywords:
Raman microspectroscopyamide-Iamide-IIIamyotrophic lateral sclerosisbend-librationphase separationsecondary structure

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Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Biophysics

Background:

  • Aggregated TAR DNA-binding protein 43 (TDP-43) forms cytosolic inclusions, a key feature in neurodegenerative diseases like ALS and FTD.
  • A leading hypothesis proposes that TDP-43 condensates mature through a liquid-to-solid transition, forming beta-sheet-rich aggregates.

Purpose of the Study:

  • To investigate the temporal and spatial dynamics of protein secondary structure changes within individual TDP-43 condensates.
  • To test the hypothesis of a liquid-to-solid transition in TDP-43 condensates using Raman spectroscopy.

Main Methods:

  • Single-condensate Raman spectroscopy was employed to monitor beta-sheet development in the C-terminal domain of TDP-43 (TDP-43CTD) in vitro.
  • Kinetic analysis of amide-I and amide-III bands tracked protein secondary structure transformation.
  • Raman mapping assessed the spatial distribution of protein density and beta-sheet content within condensates.

Main Results:

  • Condensates exhibited single-exponential kinetics for the disordered-to-beta-sheet transformation (k = 1.6 × 10^-5 s^-1).
  • Changes in the water environment, indicated by the water bend-libration band, occurred at a slower rate (k = 4.0 × 10^-6 s^-1), lagging behind protein structural changes.
  • Raman maps revealed uniform beta-sheet distribution within the condensate interior, contrasting with a central peak in protein density, challenging concentration-dependent aggregation models.
  • Spatially asymmetric beta-sheet development was observed in rare events, highlighting localized structural heterogeneity.

Conclusions:

  • The study provides insights into the temporal and spatial progression of protein structure within TDP-43 condensates.
  • The findings challenge conventional models of protein aggregation and suggest a complex maturation process.
  • Raman spectral imaging is demonstrated as a powerful tool for tracking condensate maturation dynamics at the single-condensate level.