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Establishing and Streamlining Mass Spectrometry Workflows for Elucidating Cross-links for Protein Conformational Analysis

Pearson`, Charlotte
Zaleski, Beatrice
Vitters, Ava
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Chemical crosslinking mass spectrometry (XL-MS) has emerged as a powerful tool for elucidating protein-protein interactions and structural dynamics in complex biological systems. We present a comparative analysis of two prominent software tools, Proteome Discoverer’s Xlinkx and Kojak, for the analysis of Cytochrome C cross-linked by the cleavable Disuccinimidyl Sulfoxide (DSSO). Xlinkx identified nine unique peptides and fourteen crosslinks with a minimum score cut off at 40 from cytochrome c digested with trypsin. Kojak identified significantly more peptides and crosslinks, but with much lower confidence. We visualized our data through PyMOL, mapping the distance of the three highest scoring crosslinks.
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Undergraduate
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2024-01-01
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