Enhancing protein disulfide bond cleavage by UV excitation and electron capture dissociation for top-down mass spectrometry

- UV-activation (266 nm) can homolytically cleave a disulfide bond.
- UV-activation with ECD allowed the three disulfide bonds of insulin to be cleaved.
- For proteins, combined IR/UV-activation facilitates ECD disulfide bond cleavage.
- Protein SS bonds can reform within 10-100 ms after their UV-homolytic cleavage.