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. 1994 Jun;3(6):883–887. doi: 10.1002/pro.5560030603

Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme.

M E Goldberg 1, Y Guillou 1
PMCID: PMC2142875  PMID: 8069219

Abstract

To assess the respective roles of local and long-range interactions during protein folding, the influence of the native disulfide bonds on the early formation of secondary structure was investigated using continuous-flow circular dichroism. Within the first 4 ms of folding, lysozyme with intact disulfide bonds already had a far-UV CD spectrum reflecting large amounts of secondary structure. Conversely, reduced lysozyme remained essentially unfolded at this early folding time. Thus, native disulfide bonds not only stabilize the cfinal conformation of lysozyme but also provide, in early folding intermediates, the necessary stabilization that favors the formation of secondary structure.

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Selected References

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