Analyses of Native Disulfide Bond Formations in the Early Stage of the Folding Process in Mutant Lysozymes Where the Long-Range Interactions in the Denatured State Were Modulated

Tomonori MISHIMA; Takatoshi OHKURI; Taiji IMOTO; Tadashi UEDA

doi:10.1271/bbb.70155

This article has now been updated. Please use the final version.

Analyses of Native Disulfide Bond Formations in the Early Stage of the Folding Process in Mutant Lysozymes Where the Long-Range Interactions in the Denatured State Were Modulated

Tomonori MISHIMA, Takatoshi OHKURI, Taiji IMOTO, Tadashi UEDA

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Keywords: folding, lysozyme, disulfide bond (SS bond) formation, denatured state

JOURNAL FREE ACCESS Advance online publication

Article ID: 70155

DOI https://doi.org/10.1271/bbb.70155

The final version of this article is now available: Vol. 71 (2007) , No. 8 p.2072

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Abstract

In order to clarify whether modulation of long-range interactions in the denatured state affect native disulfide bond (SS bond) formations of hen egg white lysozyme (HEL) containing a pair of cysteine residues, we examined the extent of SS bond formation among 12 variants containing a pair of cysteines. The loss of clusters 5 and 6 in the denatured state affected the formation of Cys30-115 and Cys6-127 respectively.

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