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10.1021/acs.analchem.6b03148

http://scihub22266oqcxt.onion/10.1021/acs.analchem.6b03148
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C5361889!5361889!27626298
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suck abstract from ncbi


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pmid27626298      Anal+Chem 2016 ; 88 (20): 10301-8
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  • Developing a Multiplexed Quantitative Cross-linking Mass Spectrometry Platform for Comparative Structural Analysis of Protein Complexes #MMPMID27626298
  • Yu C; Huszagh A; Viner R; Novitsky EJ; Rychnovsky SD; Huang L
  • Anal Chem 2016[Oct]; 88 (20): 10301-8 PMID27626298show ga
  • Cross-linking mass spectrometry (XL-MS) represents a recently popularized hybrid methodology for defining protein-protein interactions (PPIs) and analyzing structures of large protein assemblies. In particular, XL-MS strategies have been demonstrated to be effective in elucidating molecular details of PPIs at the peptide resolution, providing a complementary set of structural data that can be utilized to refine existing complex structures or direct de novo modeling of unknown protein structures. To study structural and interaction dynamics of protein complexes, quantitative cross-linking mass spectrometry (QXL-MS) strategies based on isotope-labeled cross-linkers have been developed. Although successful, these approaches are mostly limited to pair-wise comparisons. In order to establish a robust workflow enabling comparative analysis of multiple cross-linked samples simultaneously, we have developed a multiplexed QXL-MS strategy, namely QMIX (Quantitation of Multiplexed, Isobaric-labeled cross (X)-linked peptides) by integrating MS-cleavable cross-linkers with isobaric labeling reagents. This study has established a new analytical platform for quantitative analysis of cross-linked peptides, which can be directly applied for multiplexed comparisons of the conformational dynamics of protein complexes and protein-protein interactions at the proteome scale in future studies.
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