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Packing interactions in the apomyglobin folding intermediate

Nature Structural Biology volume 3, pages 439–445 (1996)Cite this article

Abstract

The contribution of specific packing to the stability of the sperm whale apomyoglobin intermediate has been studied by urea denaturation monitored by circular dichroism and fluorescence. Mutations disrupting native packing sites within the subdomain formed by the A, G and H helices destabilize the intermediate, in contrast to the conclusion drawn from earlier studies of pH-induced unfolding. Based on these results, the intermediate is proposed to be stabilized by both partially formed native-like tertiary, and non-specific hydrophobic interactions forming a subdomain folding intermediate. The results help to explain how the intermediate acquires its structure and stability.

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Authors and Affiliations

  1. Department of Biochemistry, Stanford University Medical Center, Stanford, California, 94305-5307, USA

    Michael S. Kay & Robert L. Baldwin

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  1. Michael S. Kay
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  2. Robert L. Baldwin
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Kay, M., Baldwin, R. Packing interactions in the apomyglobin folding intermediate. Nat Struct Mol Biol 3, 439–445 (1996). https://doi.org/10.1038/nsb0596-439

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