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ProteomicsS-Sulfenylation regulates non-enzymatic oxidative protein folding
The post-translational modification S-Sulfenylation functions as a key sensor of oxidative stress yet the dynamics of sulfenic acids in proteins is largely elusive due to it's fleeting nature. LC-MS/MS analysis has detected the evolution of this modification in oxidative and reducing states.
ORGANISM(S): Homo sapiens (Human) 
2016-12-23 | PXD004514 | Pride
Lc-ms/ms Post-translational modifications Human titin 
ProteomicsTailoring protein nanomechanics with chemical reactivity
The nanomechanical properties of elastomeric proteins determine the elasticity of a variety of tissues where modifications present at the covalent disulfide bonds can enhance protein stiffness. We propose an alternative chemical route to promote non-enzymatic oxidative protein folding via disulfide ...
ORGANISM(S): Homo sapiens (Human) 
2018-10-26 | PXD005981 | Pride
Lc-ms/ms Cysteine modifications 
UnknownContrasting the individual reactive pathways in protein unfolding and disulfide bond reduction observed within a single protein.
Not available
S-EPMC3070170 | biostudies-literature
UnknownDirect observation of an ensemble of stable collapsed states in the mechanical folding of ubiquitin.
Not available
S-EPMC2705594 | biostudies-literature
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