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7423983 
Journal Article 
The First Zero-Length Mass Spectrometry-Cleavable Cross-Linker for Protein Structure Analysis 
Hage, C; Iacobucci, C; Rehkamp, A; Arlt, C; Sinz, A; , 
2017 
Yes 
Angewandte Chemie (International Edition)
ISSN: 1433-7851
EISSN: 1521-3773 
WILEY-V C H VERLAG GMBH 
WEINHEIM 
56 
46 
14551-14555 
English 
28876504 
WOS:000414764600037 
Combining the properties of a zero-length cross-linker with cleavability by tandem mass spectrometry (MS/MS) poses great advantages for protein structure analysis using the cross-linking/MS approach. These include a reliable, automated data analysis and the possibility to obtain short-distance information of protein 3D-structures. We introduce 1,1'-carbonyldiimidazole (CDI) as an easy-to-use and commercially available, low-cost reagent that ideally fulfils these features. CDI bridges primary amines and hydroxy groups in proteins with the lowest possible spacer length of one carbonyl unit (ca. 2.6 Å). The cross-linking reaction can be conducted under physiological conditions in the pH range between 7.2 and 8. Urea and carbamate cross-linked products are cleaved upon collisional activation during MS/MS experiments generating characteristic product ions, greatly improving the unambiguous identification of cross-links. Our innovative analytical concept is exemplified and applied for bovine serum albumin (BSA), wild-type tumor suppressor p53, an intrinsically disordered protein, and retinal guanylyl cyclase activating protein-2 (GCAP-2). 
1,1′-carbonyldiimidazole; cross-linkers; mass spectrometry; protein structure; Body fluids; Chemical activation; Crosslinking; Mass spectrometry; Spectrometry; Urea; Automated data analysis; Carbonyldiimidazole; Cross-linkers; Intrinsically disordered proteins; Physiological condition; Protein structure analysis; Protein structures; Tandem mass spectrometry; Proteins; bovine serum albumin; cross linking reagent; imidazole derivative; N,N-carbonyldiimidazole; chemistry; mass spectrometry; pH; procedures; protein conformation; Cross-Linking Reagents; Hydrogen-Ion Concentration; Imidazoles; Mass Spectrometry; Protein Conformation; Serum Albumin, Bovine 
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