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Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme
Author(s) -
Goldberg Michel E.,
Guillou Yvonne
Publication year - 1994
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560030603
Subject(s) - lysozyme , folding (dsp implementation) , protein secondary structure , chemistry , circular dichroism , disulfide bond , protein folding , crystallography , protein disulfide isomerase , muramidase , biochemistry , electrical engineering , engineering
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.