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Experimental Evidence for Millisecond-Timescale Structural Evolution Following the Microsecond-Timescale Folding of a

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Small proteins fold quickly, but the villin headpiece subdomain (HP35) requires slow annealing for full folding. Time-resolved solid-state NMR revealed sidechain rearrangements occurring over milliseconds.

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Area of Science:

  • Biophysics
  • Protein dynamics
  • Structural biology

Background:

  • Small proteins are known to fold within microseconds.
  • The folding process of the villin headpiece subdomain (HP35) has not been fully characterized at the atomic level.

Purpose of the Study:

  • To investigate the folding kinetics of the 35-residue villin headpiece subdomain (HP35).
  • To identify any previously undetected slow processes involved in HP35 folding.

Main Methods:

  • Utilized time-resolved solid-state nuclear magnetic resonance (ssNMR) spectroscopy.
  • Acquired 13C ssNMR spectra of frozen HP35 solutions at 30°C after rapid cooling and before rapid freezing.
  • Employed a variable experimental time (τe) to capture dynamic changes.

Main Results:

  • Demonstrated that full folding of HP35 requires a slow annealing process.
  • Observed spectral changes on the 3-10 millisecond timescale.
  • Attributed these changes to slow protein sidechain rearrangements during the annealing phase.

Conclusions:

  • The folding of HP35 is not solely a rapid process.
  • A slow annealing mechanism, involving millisecond-timescale sidechain dynamics, is crucial for complete HP35 folding.
  • Time-resolved ssNMR is effective in detecting slow protein dynamics.