Surface Induced Dissociation Reveals Substructural Information Consistent With The Interfacial Analysis Of Protein Complexes

摘要

The results demonstrate that SID proceeds via breaking the interface of lowest area first. This is of significant impact as it is thought that in protein complex assembly pathways there is an order of association, with the largest interfaces also forming first. Furthermore, disassembly proceeds via the opposite mechanism in which the smallest interfaces are broken first. Hence SID has potential to probe disassembly and infer assembly pathways and is, therefore, a promising method for the study of protein complexes of unknown stoichiometry and structure.