At Pittcon 2024, LCGC International editor Patrick Lavery sat down with John R. Yates of the Scripps Research Institute to talk about his work in mass spectrometry and proteomics.
John R. Yates is the Ernest W. Hahn Professor at the Scripps Research Institute in La Jolla, California, specializing in Molecular Medicine & Neurobiology. He is renowned for his work in tandem mass spectrometry analysis of protein mixtures, mass spectrometry bioinformatics, and proteomics-related biological studies.
Yates is credited with inventing the SEQUEST software for correlating tandem mass spectrometry data with sequences in databases and pioneering the shotgun proteomics technique for analyzing protein mixtures. His laboratory has developed proteomic methods for studying protein complexes, posttranslational modifications, organelles, and quantitative protein expression analysis.
Click here for a recap of Yates' lecture from this year's Pittcon.
Yates has received numerous awards, including the ASMS Biemann Medal, HUPO Achievement Award, Christian Anfinsen Award (Protein Society), Analytical Chemistry Award (ACS), Ralph N. Adams Award, Thomson Medal (IMSF), John B. Fenn Award (ASMS), and HUPO Discovery Award. Currently, he serves as the editor-in-chief of the Journal of Proteome Research.
LCGC International sat down with Yates at Pittcon, held this year a short drive from La Jolla in San Diego, to discuss the following topics:
Study Explores Thin-Film Extraction of Biogenic Amines via HPLC-MS/MS
March 27th 2025Scientists from Tabriz University and the University of Tabriz explored cellulose acetate-UiO-66-COOH as an affordable coating sorbent for thin film extraction of biogenic amines from cheese and alcohol-free beverages using HPLC-MS/MS.
Quantifying Microplastics in Meconium Samples Using Pyrolysis–GC-MS
March 26th 2025Using pyrolysis-gas chromatography and mass spectrometry, scientists from Fudan University and the Putuo District Center for Disease Control and Prevention detected and quantified microplastics in newborn stool samples.
Multi-Step Preparative LC–MS Workflow for Peptide Purification
March 21st 2025This article introduces a multi-step preparative purification workflow for synthetic peptides using liquid chromatography–mass spectrometry (LC–MS). The process involves optimizing separation conditions, scaling-up, fractionating, and confirming purity and recovery, using a single LC–MS system. High purity and recovery rates for synthetic peptides such as parathormone (PTH) are achieved. The method allows efficient purification and accurate confirmation of peptide synthesis and is suitable for handling complex preparative purification tasks.