StavroX

StavroX analyzes peptide–peptide cross-links from chemical crosslinking coupled to mass spectrometry (MS) and tandem mass spectrometry (MS/MS) to derive structural and interaction information for proteins and protein complexes.

Key Features:

• Handling Complex Crosslinking Datasets: Processes large and highly complex crosslinking datasets generated after chemical crosslinking and enzymatic digestion.
• Automated MS and MS/MS Analysis: Performs automated analysis of MS and MS/MS data to detect and evaluate peptide–peptide cross-links.
• Structural Information Extraction: Derives low-resolution structural constraints and interaction information from crosslinking-MS data.

Scientific Applications:

• Low-resolution structural analysis of proteins and complexes: Derives low-resolution structural information from chemical crosslinking combined with MS.
• Protein–protein interaction studies (calmodulin–Munc13 peptide): Applied to analyze the complex between calmodulin and a peptide derived from Munc13.
• Structural analysis of protein fragments (N-terminal ß-laminin fragment): Provided structural insights into an N-terminal ß-laminin fragment.
• Complex formation studies (guanylyl cyclase activating protein-2 and retinal guanylyl cyclase peptide): Used to study the interaction between guanylyl cyclase activating protein-2 and a peptide derived from retinal guanylyl cyclase.

Methodology:

Automated computational analysis of MS and MS/MS datasets derived from chemical crosslinking (post-enzymatic digestion) to handle large datasets and extract structural and interaction information about peptide–peptide cross-links.