The susceptibility of disulfide bonds towards radiation damage may be explained by S⋯O interactions.

ABSTRACT: Radiation-induced damage to protein crystals during X-ray diffraction data collection is a major impediment to obtaining accurate structural information on macromolecules. Some of the specific impairments that are inflicted upon highly brilliant X-ray irradiation are metal-ion reduction, disulfide-bond cleavage and a loss of the integrity of the carboxyl groups of acidic residues. With respect to disulfide-bond reduction, previous results have indicated that not all disulfide bridges are equally susceptible to damage. A careful analysis of the chemical environment of disulfide bonds in the structures of elastase, lysozyme, acetylcholinesterase and other proteins suggests that S-S bonds which engage in a close contact with a carbonyl O atom along the extension of the S-S bond vector are mor

SUBMITTER: Bhattacharyya R 

PROVIDER: S-EPMC7467163 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature