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


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. Study holds ProTherm entries: 8650 Extra Details: molten globule; temperature jump; fluorescence; circular dichroism

Submission Details

ID: VVhviJYA3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:36 p.m.

Version: 1

Publication Details
Ballew RM;Sabelko J;Gruebele M,Proc. Natl. Acad. Sci. U.S.A. (1996) Direct observation of fast protein folding: the initial collapse of apomyoglobin. PMID:8650166
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