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SPR-MS in functional proteomics.

Jos Buijs¹, Gary C Franklin

¹Biacore AB, Rapsgatan 7, 754 50 Uppsala, Sweden. Jos.Buijs@Biacore.com

Briefings in Functional Genomics & Proteomics

|June 25, 2005

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Combining surface plasmon resonance (SPR) and mass spectrometry (MS) offers a powerful tool for functional proteomics. This integrated approach identifies proteins based on binding criteria, advancing cellular process and interaction studies.

Area of Science:

Proteomics
Biochemistry
Analytical Chemistry

Background:

Mapping protein networks and understanding protein functions in cellular processes is a significant challenge in proteomics.
Traditional methods often struggle to comprehensively link protein interactions with their functional outcomes.

Purpose of the Study:

To highlight the synergistic capabilities of combining surface plasmon resonance (SPR) with mass spectrometry (MS) for advanced functional proteomics.
To review recent developments and applications of integrated SPR-MS technologies.

Main Methods:

Affinity purification, quantification, and interaction characterization of proteins using SPR.
Identification and structural characterization of biomolecules using MS.
Integrated SPR-MS/MS for detailed analysis, including ligand fishing and post-translational modifications.

Related Experiment Videos

Main Results:

Demonstrated the ability to identify proteins based on functional binding criteria through combined SPR-MS.
Showcased applications in ligand fishing, peptide sequencing, and post-translational modification analysis.
Validated the utility of SPR-MS in enzyme inhibitor screening.

Conclusions:

The integrated SPR-MS approach provides a unique and powerful analytical tool for functional proteomics.
This combined technology enables precise identification and characterization of proteins and their interactions.
SPR-MS significantly advances the investigation of cellular processes and protein functions.