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Submillisecond folding of monomeric lambda repressor

G S Huang1, T G Oas

  • 1Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.

Proceedings of the National Academy of Sciences of the United States of America
|July 18, 1995
PubMed
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The folding kinetics of phage lambda repressor fragment [lambda 6-85] were studied using dynamic NMR. This protein folds exceptionally fast, with all folding events occurring on the submillisecond timescale.

Area of Science:

  • Biophysics
  • Protein folding dynamics
  • Nuclear Magnetic Resonance (NMR) spectroscopy

Background:

  • The N-terminal domain of phage lambda repressor (lambda 6-85) is known to fold via a two-state mechanism.
  • Understanding protein folding kinetics is crucial for deciphering protein function and dysfunction.

Purpose of the Study:

  • To investigate the folding kinetics of the truncated phage lambda repressor N-terminal domain (lambda 6-85).
  • To determine the folding and unfolding rates and their dependence on urea concentration.
  • To explore the implications of rapid folding on protein structure and dynamics.

Main Methods:

  • Dynamic Nuclear Magnetic Resonance (NMR) spectroscopy was employed to monitor folding.
  • Simulation of exchange-broadened aromatic resonances of Tyrosine-22 (Tyr-22) allowed rate determination.

Related Experiment Videos

  • Experiments were conducted across a range of urea concentrations (1.35 to 3.14 M) at 37°C.

    • Main Results:

    • The folding and unfolding rates of lambda 6-85 were determined to be 3600 ± 400 s⁻¹ and 27 ± 6 s⁻¹, respectively, at 0 M urea.
    • The folding rate constant of lambda 6-85 is significantly faster (14-54 fold) than other fast-folding globular proteins.
    • The transition state for the rate-determining step appears to be highly exposed to solvent.

    Conclusions:

    • Phage lambda repressor fragment lambda 6-85 exhibits remarkably rapid folding and unfolding kinetics.
    • The all-helical secondary structure may contribute to the protein's fast folding.
    • Fundamental protein folding events can occur on the submillisecond timescale.