title: Development of Large-scale Cross-linking Mass Spectrometry.
abstract: Cross-linking mass spectrometry (CLMS) provides distance constraints to study the structure of proteins, multiprotein complexes and protein-protein interactions which are critical for the understanding of protein function. CLMS is an attractive technology to bridge the gap between high-resolution structural biology techniques and proteomic-based interactome studies. However, as outlined in this review there are still several bottlenecks associated with CLMS which limit its application on a proteome-wide level. Specifically, there is an unmet need for comprehensive software that can reliably identify cross-linked peptides from large data sets. In this review we provide supporting information to reason that targeted proteomics of cross-links may provide the required sensitivity to reliably detect and quantify cross-linked peptides and that a reporter ion signature for cross-linked peptides may become a useful approach to increase confidence in the identification process of cross-linked peptides. In addition, the review summarizes the recent advances in CLMS workflows using the analysis of condensin complex in intact chromosomes as a model complex.
authors.affiliation: From the ‡Division of Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden helena.barysz@gmail.com.
authors.forename: Helena Maria
authors.initials: HM
authors.lastname: Barysz
authors.affiliation: From the ‡Division of Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden.
authors.forename: Johan
authors.initials: J
authors.lastname: Malmström
mesh_terms: D013058:Mass Spectrometry; D010455:Peptides; D025941:Protein Interaction Mapping; D040901:Proteomics
chemical_list: D010455:Peptides