WELCOME TO THE LOO LAB FOR
MASS SPECTROMETRY
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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.
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. Click below for more information!
research
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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, including a wide array of neurodegenerative diseases.
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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.
research features
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Top-down mass spectrometry and assigning internal fragments for determining disulfide bond positions in proteins.
https://doi.org/10.1039/D2AN01517J
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Impact of Internal Fragments on Top-Down Analysis of Intact Proteins by 193 nm UVPD.
https://doi.org/10.1021/acs.jproteome.2c00583
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Native Top-Down Mass Spectrometry with Collisionally Activated Dissociation Yields Higher-Order Structure Information for Protein Complexes.
https://doi.org/10.1021/jacs.2c06726
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Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43.
https://doi.org/10.1038/s41586-022-04670-9
lab members
principal investigator
Joseph Loo
principal investigator
Rachel Loo
Benqian Wei
graduate student
graduate student
Boyu Zhao
Giang (Jessie) Lee
graduate student
graduate student
Andrew Goring
Eileen J. Olivares
graduate student
Merin Rixen
graduate student
Megan Hong
graduate student
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September 2023Congrats Joe on receiving the ACS 2024 Frank H. Field and Joe L. Franklin Award for Outstanding Achievement in Mass Spectrometry!
Congrats Merin and Eileen on being appointed as gBSA board members for 2023-2024! Merin has assumed the role of co-president. Eileen will continue her role as treasurer. -
July 2023Congrats Andrew on being awarded the Whitcome Pre-doctoral Fellowship in Molecular Biology for 2023-24!
Welcome Matt! Matt will be rotating in the Loo Lab for the Summer. -
June 2023Congrats Eileen on passing your oral qualifying exam!
Ben's and Carter's work on Top-Down Mass Spectrometry of Intact Monoclonal Antibodies and Antibody−Drug Conjugates has been published in Analytical Chemistry (https://doi.org/10.1021/acs.analchem.3c01426)! -
May 2023Congrats Ben on being awarded a 2023 ACS Division of Analytical Chemistry Graduate Fellowship, sponsored by Agilent.
Congrats Merin on passing your oral qualifying exam!
Welcome Toy! Toy has joined the Loo lab!
Welcome Megan! Megan has joined the Loo lab! She will be co-mentored by Dr. Gal Bitan!