Investigation of phycobilisome subunit interaction interfaces by coupled cross-linking and mass spectrometry.

@article{Tal2014InvestigationOP,
  title={Investigation of phycobilisome subunit interaction interfaces by coupled cross-linking and mass spectrometry.},
  author={Ofir Tal and Beny Trabelcy and Yoram Gerchman and Noam Adir},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 48},
  pages={33084-97}
}
The phycobilisome (PBS) is an extremely large light-harvesting complex, common in cyanobacteria and red algae, composed of rods and core substructures. These substructures are assembled from chromophore-bearing phycocyanin and allophycocyanin subunits, nonpigmented linker proteins and in some cases additional subunits. To date, despite the determination of crystal structures of isolated PBS components, critical questions regarding the interaction and energy flow between rods and core are still… CONTINUE READING