Direct observation of fast protein folding: The initial collapse of apomyoglobin

R. M. Ballew, J. Sabelko, M. Gruebele

Research output: Contribution to journalArticlepeer-review


The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state are observed and are complete in under 20 μs. Experiments on mutants and consideration of steady-state CD and fluorescence spectra indicate that the observed microsecond phase monitors assembly of an A·(H·G) helix subunit. Measurements at different viscosities indicate diffusive behavior even at low viscosities, in agreement with motions of a solvent-exposed protein during the initial collapse.

Original languageEnglish (US)
Pages (from-to)5759-5764
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number12
StatePublished - Jun 11 1996


  • circular dichroism
  • fluorescence
  • molten globule
  • temperature jump

ASJC Scopus subject areas

  • General


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