MS-Spectre

MS-Spectre analyzes LC-MS and LC-MS/MS mzXML data to perform quantitative proteomics and to characterize protease cleavage patterns and N-glycosylation from mass spectrometry datasets.

Key Features:

• Data Compatibility: Supports mzXML files from LC-MS and LC-MS/MS experiments.
• Quantitative Analysis: Implements algorithms to extract quantitative protein- and peptide-level information across multiple samples.
• Protease Activity Evaluation: Analyzes cleavage patterns to assess specificity and activity of proteases, including the acidic prolyl endoprotease from Aspergillus niger.
• Glycoprotein Analysis: Detects and characterizes N-glycosylation sites and related glycopeptide features using tandem MS data.
• Cleavage Specificity Assessment: Evaluates cleavage specificity from in-solution digests of standard proteins and protein digests.
• Post-Source Decay Analysis: Performs post-source decay analysis to support peptide fragmentation confirmation.

Scientific Applications:

• Proteomics Research: Quantitative analysis and characterization of proteins from LC-MS(/MS) datasets for proteomic studies.
• Enzyme Characterization: Characterization of enzyme specificity, activity, and behavior, exemplified by studies of the prolyl endoprotease from Aspergillus niger.
• Glycoprotein Studies: Identification and characterization of N-glycosylation sites and their roles in glycoprotein research.

Methodology:

Processes mzXML LC-MS(/MS) data with algorithms to extract quantitative information, performs spectral analysis including MALDI-TOF/TOF tandem MS integration and post-source decay analysis, and analyzes cleavage patterns from in-solution and protein digests.