S-Sulfenylation regulates non-enzymatic oxidative protein folding
Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Velos
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: 
Steven Lynham
LAB HEAD: Sergi Garcia-Manyes
PROVIDER: PXD004514 | Pride | 2016-12-23
REPOSITORIES: Pride
Publications
Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding.
Beedle Amy E M AE Lynham Steven S Garcia-Manyes Sergi S
Nature communications 20160822
The post-translational modification S-sulfenylation functions as a key sensor of oxidative stress. Yet the dynamics of sulfenic acid in proteins remains largely elusive due to its fleeting nature. Here we use single-molecule force-clamp spectroscopy and mass spectrometry to directly capture the reactivity of an individual sulfenic acid embedded within the core of a single Ig domain of the titin protein. Our results demonstrate that sulfenic acid is a crucial short-lived intermediate that dictate ...[more]
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