Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872973 | FEBS Letters | 2005 | 4 Pages |
Abstract
This study explores how the kinetics of a coupled folding/binding reaction depend on the initial conformation of the protein. Stopped-flow spectroscopy is used to monitor the reaction of apo-myoglobin (aMb) with hemin dicyanide at pH 7.2. Different initial aMb conformations are tested. In the case of acid-denatured aMb, the observed kinetics are consistent with a “fly-casting” scenario [Shoemaker et al., Proc. Natl. Acad. Sci. USA 97 (2000) 8868-8873]. However, the formation of a compact complex proceeds more rapidly in the case of prefolded aMb. This finding is opposite to what would be expected based on predictions of the fly-casting model.
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Authors
Marcelo O. Crespin, Brian L. Boys, Lars Konermann,