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Nat Struct Biol. 2001 Jan;8(1):68-72.

Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate.

Author information

1
School of Biochemistry and Molecular Biology and the Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.

Abstract

Many proteins populate partially organized structures during folding. Since these intermediates often accumulate within the dead time (2-5 ms) of conventional stopped-flow and quench-flow devices, it has been difficult to determine their role in the formation of the native state. Here we use a microcapillary mixing apparatus, with a time resolution of approximately 150 micros, to directly follow the formation of an intermediate in the folding of a four-helix protein, Im7. Quantitative kinetic modeling of folding and unfolding data acquired over a wide range of urea concentrations demonstrate that this intermediate ensemble lies on a direct path from the unfolded to the native state.

PMID:
11135674
DOI:
10.1038/83074
[Indexed for MEDLINE]

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