title: The advancement of chemical cross-linking and mass spectrometry for structural proteomics: from single proteins to protein interaction networks.
abstract: During the last 15 years, chemical cross-linking combined with mass spectrometry (MS) and computational modeling has advanced from investigating 3D-structures of isolated proteins to deciphering protein interaction networks. In this article, the author discusses the advent, the development and the current status of the chemical cross-linking/MS strategy in the context of recent technological developments. A direct way to probe in vivo protein-protein interactions is by site-specific incorporation of genetically encoded photo-reactive amino acids or by non-directed incorporation of photo-reactive amino acids. As the chemical cross-linking/MS approach allows the capture of transient and weak interactions, it has the potential to become a routine technique for unraveling protein interaction networks in their natural cellular environment.
authors.affiliation: Department of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin-Luther University Halle-Wittenberg, Wolfgang-Langenbeck-Straße 4, D-06120 Halle (Saale), Germany.
authors.forename: Andrea
authors.initials: A
authors.lastname: Sinz
mesh_terms: D000596:Amino Acids / Q000737:chemistry / Q000235:genetics; D000818:Animals; D019295:Computational Biology; D003432:Cross-Linking Reagents / Q000737:chemistry*; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D019920:Photoaffinity Labels / Q000737:chemistry; D025941:Protein Interaction Mapping; D055503:Protein Multimerization; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D040901:Proteomics
chemical_list: D000596:Amino Acids; D003432:Cross-Linking Reagents; D019920:Photoaffinity Labels; D011506:Proteins
keywords: chemical cross-linking; mass spectrometry; protein 3D-structure; protein networks; unnatural amino acids