Disulfide bonds as switches for protein function
Abstract
The prevailing view is that disulfide bonds have been added during evolution to enhance the stability of proteins that function in a fluctuating cellular environment. However, recent evidence indicates that disulfide bonds can be more than inert structural motifs. The function of some secreted soluble proteins and cell-surface receptors is controlled by cleavage of one or more of their disulfide bonds; this cleavage is mediated by catalysts or...
Paper Details
Title
Disulfide bonds as switches for protein function
Published Date
Apr 1, 2003
Volume
28
Issue
4
Pages
210 - 214
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