Ontology highlight
ABSTRACT:
SUBMITTER: Yi MC
PROVIDER: S-EPMC4899241 | biostudies-literature | 2016 Jun
REPOSITORIES: biostudies-literature
Yi Michael C MC Khosla Chaitan C
Annual review of chemical and biomolecular engineering 20160317
Disulfide bonds represent versatile posttranslational modifications whose roles encompass the structure, catalysis, and regulation of protein function. Due to the oxidizing nature of the extracellular environment, disulfide bonds found in secreted proteins were once believed to be inert. This notion has been challenged by the discovery of redox-sensitive disulfides that, once cleaved, can lead to changes in protein activity. These functional disulfides are twisted into unique configurations, lea ...[more]