Evaluating the performance of an ETD-cleavable cross-linking strategy for elucidating protein structures.

ABSTRACT: Chemical cross-linking is a powerful strategy for elucidating the structures of protein or protein complexes. The distance constraints obtained from cross-linked peptides represent the three-dimensional structures of the protein complexes. Unfortunately, structural analysis using cross-linking approach demands a significant amount of data to elucidate protein structures. This requires the development of several cleavable cross-linkers with different range of spacer chains. An Electron Transfer Dissociation (ETD) tandem mass spectrometry cleavable bond hydrazone was reported. Its fragmentation with conjugated peptides showed promise for the development of a new ETD cleavable cross-linker. However, no cross-linker was developed utilizing this ETD cleavable bond. For the first time, we attemp

SUBMITTER: Chakrabarty JK 

PROVIDER: S-EPMC7377963 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature