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. 1996 Jun 11;93(12):5759-64.
doi: 10.1073/pnas.93.12.5759.

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

R M Ballew  1 , J Sabelko, M Gruebele
Affiliations

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

R M Ballew et al. Proc Natl Acad Sci U S A. .

Abstract

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 micros. Experiments on mutants and consideration of steady-state CD and fluorescence spectra indicate that the observed microsecond phase monitors assembly of an A x (H x 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.

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