Identification of Disulfide-Containing Chemical Cross-Links in Proteins Using MALDI-TOF/TOF-Mass Spectrometry
作者： Gordon J. King , Alun Jones , Bostjan Kobe , Thomas Huber , Dmitri Mouradov
DOI: 10.1021/AC702277Q
关键词:
摘要: Cross-linking can be used to identify spatial relationships between amino acids in proteins or protein complexes. A rapid and sensitive method for identifying the site of cross-linking using dithiobis(sulfosuccinimidyl propionate) (DTSSP) is presented illustrated with experiments murine cortactin, actin acyl-CoA thioesterase. characteristic 66 Da doublet, which arises from asymmetric fragmentation disulfide DTSSP-modified peptides, observed mass spectra obtained under MALDI-TOF/TOF-MS conditions allows assignment cross-links modified proteins. This doublet not only linear cross-linked peptides but also cyclic when simultaneous peptide backbone occurs. We suggest a likely mechanism this fragmentation. use guanidinylation O-methyl isourea extend coverage MAL...
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