Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II

Protein cross-linking and radiolytic footprinting coupled with high-resolution mass spectrometry were used to examine the structure of PsbP and PsbQ when they are bound to Photosystem II. In its bound state, the N-terminal 15-amino-acid residue domain of PsbP, which is unresolved in current crystal...

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Publicado en:Proc Natl Acad Sci U S A
Autores principales: Mummadisetti, Manjula P., Frankel, Laurie K., Bellamy, Henry D., Sallans, Larry, Goettert, Jost S., Brylinski, Michal, Limbach, Patrick A., Bricker, Terry M.
Formato: Artigo
Lenguaje:Inglês
Publicado: National Academy of Sciences 2014
Materias:
Biological Sciences
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC4234589/
https://ncbi.nlm.nih.gov/pubmed/25349426
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1415165111
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