SEATTLE, WA—Holding her breath as the analytical balance stabilized Monday morning, University of Washington graduate student Aubrey Smith, 27, experienced a fleeting moment of pure joy as the digital...

Tenure-Track Assistant Professor in Organic Chemistry. The Department of Chemistry and Biochemistry at the College of Charleston invites applications for a tenure-track faculty position beginning in F...

The agonistic activity of IgG2 antibodies depends, in part, on the flexibility of their hinge region, which is slow to measure in full-length antibodies. Here, the authors develop a rapid mass spectro...

Postdoctoral Researcher The Kenagy Lab (Department of Chemistry; https://kenagy.chem.umn.edu/) and the Millet Lab (Department of Soil, Water, and Climate; https://atmoschem.umn.edu) at the University ...

Journal of the American Chemical SocietyDOI: 10.1021/jacs.5c21227

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The ACS Division of Analytical Chemistry is pleased to announce the recipients of the 2026 Division Awards. ACS Division of Analytical Chemistry Award in Electrochemistry

Covalent ligands are widely used to label, probe, and modulate proteins, but peptide-centric readouts obscure how modifications colocalize on intact proteoforms. This can limit insight into ligand mechanism, modification stoichiometry, and the architecture of multisite protein conjugates. We present a general native top-down mass spectrometry workflow that quantifies electrophile reactivity directly on intact proteins. Using NHS esters as a model electrophile class, we apply a deconvolution framework to infer differential reactivity at primary amines across promiscuous, multisite modification patterns. The approach preserves full modification connectivity, avoids sample-preparation artifacts associated with denaturation and digestion, and should extend to electrophiles with unknown reactivity. Overall, this framework provides a general platform for designing covalent therapeutics, bioconjugates, and activity-based probes with proteoform-level resolution.

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Electrospray ionization (ESI)-based native mass spectrometry (MS) has been extensively used to study non-covalent protein complexes and their structural aspects in the gas phase. As such it has a stable place in the portfolio of modern structural biology and biopharmaceutical analysis techniques. It is also promising as an approach to deliver pro-teins and their assemblies into the gas phase for single particle experiments at advanced light sources such as free electron lasers and synchrotrons. Here we report on a novel radiofrequency ion transfer interface enabling gas flow laminarization at low pressure for efficient capture, focusing, thermalization, trapping and gating of ions into a mass analyser, boosting up to 19-fold the observable signal intensities especially for notoriously challenging multi-megadalton assemblies such as in-tact viral capsids. The new ion transfer interface offers unique opportunities for interdisciplinary approaches intersecting native MS-guided structural biology, molecular and cluster physics as well as (bio)analytical applications. Additionally, when combined with sensitive detection of individual particles, this technology could eventually also open new avenues in clinical diagnostics, enabling for example the analysis of viruses at very low concentrations directly from dilute patient-derived samples as well as viral therapeutic vectors along the biopharmaceutical production chain, thereby helping to un-lock the full potential of native MS.

Publication date: Available online 8 January 2026 Source: International Journal of Mass Spectrometry Author(s): Lasini Amunugama, Jared B. Shaw

Harvard University has announced that it's suing the Trump administration to halt a freeze on more than $2.2 billion in grants after the institution said it would defy the Trump administration’s demands to limit activism on campus.

Cross-linking and covalent labeling are common tools for protein structural elucidation by mass spectrometry. However, despite the importance of electrostatic interactions in proteins, there are not m...

🔊 Mass spectrometry post-doc position in Switzerland Join our dynamic and interdisciplinary team for a post-doc in Geneva, Switzerland, where we develop advanced mass spectrometry methods for biophysi...