Abstract

Viruses affect basically all organisms on earth. Some are detrimental to human development, whereas those targeting pathogenic bacteria or crop pathogens can be beneficial for us. An integral part of icosahedral viruses is the capsid protein shell protecting the genome. Many copies of the capsid protein often self-assemble into shells of defined size. Low binding affinity of individual subunits allows efficient assembly and gives rise to highly stable particles. These capsids can be studied by native and hydrogen/deuterium exchange mass spectrometry (MS) in terms of stoichiometry, dynamics, assembly pathways and stability.

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