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© Research
Publication : Protein science : a publication of the Protein Society

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Protein science : a publication of the Protein Society - 01 Jun 1994

Goldberg ME, Guillou Y

Link to Pubmed [PMID] – 8069219

Protein Sci. 1994 Jun;3(6):883-7

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.

https://www.ncbi.nlm.nih.gov/pubmed/8069219