The Loo Lab

Research

The research interests of Professor Loo's group include the development and application of bioanalytical methods for the structural characterization of proteins and post-translational modifications, proteomics-based research, and the elucidation of protein biomarkers to aid human health studies. Advanced mass spectrometry and protein separation methods are central tools for the lab.

Structural Biology

Protein-protein and protein-ligand interactions are involved in most biological machineries. The characterization of these interactions using mass spectrometry (MS) and ion mobility spectrometry (IMS) has great advantages over other technologies because of its high sensitivity and its potential to provide stoichiometry and structure information for large protein complexes, including membrane proteins. Protein-drug interactions are being probed using MS tools to aid our research in neurodegenerative diseases.

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Proteomics

Mass spectrometry-based proteomics is used for protein profiling to gain a better understanding of complex biological systems. New proteomics platforms and sample preparation methods can improve the speed and dynamic range for measuring proteins in both qualitative and quantitative fashions. Proteomics can contribute to drug discovery efforts to identify new protein targets and to identify new biomarkers of human diseases and conditions.

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MICROBIAL PROTEINS AND THEIR MODIFICATIONS

As a member of the UCLA-DOE Institute for Genomics and Proteomics, we apply LC-MS-based proteomics to elucidate biological pathways relevant to biofuel production. We have discovered the importance of protein post-translational modifications to metabolic regulation within microbial consortia. Proteomics serves to elucidate the surface layer (S-Layer) of archaea and prokaryotes and gives clues to how the surface layer plays a critical role in microbial survival.

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