✦ LIBER ✦

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

✍ Scribed by Michel E. Goldberg; Yvonne Guillou

Publisher: Cold Spring Harbor Laboratory Press
Year: 2008
Tongue: English
Weight: 512 KB
Volume: 3
Category: Article
ISSN: 0961-8368
DOI: 10.1002/pro.5560030603

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✦ Synopsis

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 final conformation of lysozyme but also provide, in early folding intermediates, the necessary stabilization that favors the formation of secondary structure.

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