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The present technology identifies how protein tertiary structures can be determined from IMS-MS data in an automated manner.
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Summary: Ion mobility spectrometry-mass spectrometry (IMS-MS) is ideally suited to study co-existing, transient conformations of proteins and their complexes related to diseases because of its high sensitivity and speed of MS analysis. Many existing results suggest that IMS-MS could accurately elucidate structures for these protein conformations in a high-throughput manner. The present technology identifies how protein tertiary structures can be determined from IMS-MS data in an automated manner. Advantages: IMS-MS requires a fraction of sample amounts and time Does not suffer from charge-state dependent protein dynamics in the gas phase Computationally efficient Automatized