Join us for a fascinating conversation with Dr. Subhoja Chakraborty from the University of Central Florida, whose cutting-edge research targets the global challenge of malaria drug resistance. Dr. Chakraborty shares her journey from structure-based drug design during her PhD to her recent collaborative work repurposing human kinase inhibitors as rapid, selective antimalarials against drug-resistant Plasmodium falciparum strains.<h4>In this episode, you'll learn:</h4><ul><li>How structure-guided approaches reveal potential drug targets, including cysteine proteases like falcipain-2, and kinases implicated in malaria's complex life cycle.</li><li>The power of repurposing kinase inhibitors originally developed for cancer and other diseases, focusing on compound 12, which blocks hemozoin formation and protein kinase 6—key steps in parasite survival.</li><li>Lab techniques such as affinity, gel filtration, and size exclusion chromatography for recombinant protein purification—and how troubleshooting is crucial for high-yield, stable complexes.</li><li>Advances in mass spectrometry for characterizing protein interactions, validating drug targets, and mapping molecular pathways pivotal to malaria therapeutics.</li><li>Tips and lessons for new researchers facing the challenges of sample preparation, complex protocols, and working as part of a collaborative team.</li></ul>Dr. Chakraborty’s insights bridge the gap between basic science and translational drug discovery, offering hope for more effective, targeted malaria treatments in a world where resistance to frontline therapies threatens millions.<h4>Referenced Papers:</h4><ul><li>"Plasmodium falciparum protein kinase 6 and hemozoin formation are inhibited by a type II human kinase inhibitor exhibiting antimalarial activity" (Cell Chemical Biology, 2025)</li><li>"New insights of falcipain 2 structure from Plasmodium falciparum 3D7 strain" (BBRC, 2022)</li><li>"Structure-Based Optimization of Protease−Inhibitor Interactions to Enhance Specificity of Human Stefin‑A against Falcipain‑2 from the Plasmodium falciparum 3D7 Strain" (Biochemistry, 2023)</li></ul>If you’re a student, scientist, or simply passionate about advances in infectious disease research, this episode offers actionable insights, inspiring advice, and a front-row seat to innovation in combating malaria.<h3>Video Transcription</h3><h4>From Structural Biology to Drug Discovery: Chromatography and Mass Spectrometry in Malaria Research</h4><h5>Introduction</h5>In this discussion, Subhoja shares insights into her research journey, focusing on malaria drug discovery and the role of modern analytical techniques in biological and biomedical research. The conversation is aimed primarily at undergraduate students and early-career researchers interested in chemistry, biotechnology, and life sciences.<h5>Research Focus: Malaria Drug Discovery and Kinase Targets</h5>Subhoja is currently involved in malaria drug discovery research at the University of Central Florida, where she has been working since beginning her postdoctoral position two years ago. Her earlier PhD research focused on structure-based drug design in malaria, using a combination of in silico approaches, recombinant protein expression, and X-ray crystallography to determine precise three-dimensional structures of target proteins and their inhibitors.This structural perspective provided a foundation for her current work, which centers on drug discovery through compound screening and repurposing. A recent publication from her laboratory explores the use of repurposed mammalian CDK-like kinase inhibitors as potential antimalarial agents. While such kinase inhibitors are well known in cancer and cardiovascular research, their application to malaria targets represents a novel and promising approach.Kinases are attractive drug targets because of their central role in cell signaling and growth pathways. By targeting specific kinases involved in different stages of the malaria parasite life cycle—whether asexual growth, gametocytogenesis, or differentiation—it may be possible to significantly inhibit parasite growth and progression.<h5>Chromatography in Protein Expression and Purification Workflows</h5>Chromatography plays a critical role throughout Subhoja’s research. Her experience spans from basic chromatography techniques during her early training to advanced protein purification workflows using affinity chromatography, gel filtration (size exclusion chromatography), and ion exchange chromatography.Recombinant proteins are routinely purified using affinity resins such as nickel or cobalt, followed by further purification to remove contaminants. Fast Protein Liquid Chromatography (FPLC) enables compact, stepwise purification workflows suitable for producing proteins for in vitro assays.A recurring challenge in this process is the expression of high-molecular-weight proteins, which often accumulate in insoluble fractions or inclusion bodies. Careful selection of expression vectors, host systems, and induction conditions is therefore essential to maximize yield and solubility.<h5>Integrating Size Exclusion Chromatography into the Workflow</h5>Size exclusion chromatography (SEC) is typically used after affinity purification to further improve protein purity. Following elution with imidazole or glutathione, desalting is required to prevent buffer components from interfering with downstream assays. This is often achieved using desalting columns such as G-25 or PD-10.To remove lower-molecular-weight contaminants, finer SEC media—such as Superdex or Sephacryl columns—are employed. Concentration steps using molecular-weight cut-off filters are then applied to obtain the desired protein concentration for functional studies.These iterative purification and troubleshooting steps are a routine part of protein biochemistry and reflect the importance of methodical optimization and careful validation.<h5>The Role of Mass Spectrometry in Biomolecular Characterization</h5>Mass spectrometry is a key analytical tool in Subhoja’s research pipeline, particularly for target identification and validation. In both malaria and cancer research, MS is used alongside chromatography, immunoprecipitation, and pull-down assays to study protein interactions and molecular recognition events.Affinity-based mass spectrometry enables the identification of binding partners and interactors, whether studying proteins, long non-coding RNAs, or protein complexes. Techniques such as native MS, tandem affinity purification, and proximity labeling (e.g., TurboID-based workflows) provide deeper insights into molecular networks and signaling pathways.These approaches are essential for understanding how candidate drug targets function within complex biological systems.<h5>Sample Preparation Challenges in Biological Research</h5>Sample preparation remains one of the most challenging aspects of biological experimentation. Whole-cell lysates contain proteases, nucleases, and other components that can rapidly degrade target molecules. Preventing degradation requires minimizing preparation time, maintaining low temperatures, and using appropriate inhibitor cocktails.Reproducibility is also critical: biological experiments require multiple replicates, and variability is often unavoidable. Careful handling, protocol optimization, and continuous troubleshooting are essential to ensure reliable results, whether preparing samples for chromatography, mass spectrometry, sequencing, or immunoprecipitation.<h5>Advances in Chromatography and MS for Malaria Research</h5>Modern advances in chromatography and mass spectrometry significantly enhance malaria research by enabling precise target identification, quantification, and functional characterization. Drug discovery workflows begin with construct design and recombinant expression, followed by purification and interaction studies.In malaria research, stage-specific parasite biology requires careful extraction and analysis of proteins from different life cycle stages. Tandem affinity MS, immunoprecipitation, and in vivo validation studies help confirm target relevance and therapeutic potential.Recent work on repurposed kinase inhibitors has shown promising results, including inhibition of hemozoin formation—a key detoxification pathway for the malaria parasite—highlighting the potential of such compounds for further development.<h5>Malaria, Drug Resistance, and Global Impact</h5>Malaria remains a major global health burden, with over 600,000 deaths annually and widespread drug resistance complicating treatment. Artemisinin resistance, particularly associated with mutations in the K13 propeller domain, has driven the search for new targets and therapies.During her PhD, Subhoja focused on falcipain-2, a cysteine protease involved in hemoglobin degradation within the parasite. This pathway is critical for parasite survival and has emerged as a promising drug target. Her work revealed that falcipain-2 operates within a larger protein complex responsible for hemoglobin processing and amino acid release.Understanding these molecular mechanisms is essential for developing robust, stage-specific antimalarial strategies.<h5>Advice for Early-Career Researchers</h5>For researchers just starting out, Subhoja emphasizes the importance of hands-on experience. Working directly with cells, lysates, and analytical tools is essential for truly understanding experimental systems. Failure is an inherent part of research, and perseverance is key.Motivation, teamwork, careful sample handling, and thorough preparation all contribute to long-term success. Reading extensively, critically evaluating one’s own work, and appreciating incremental progress are vital aspects of a sustainable research career.Every successful experiment—no matter how small—represents meaningful progress and contributes to the broader goals of science and medicine.<h5>Closing Remarks</h5>The discussion highlights how interdisciplinary approaches combining chromatography, mass spectrometry, structural biology, and biochemistry are driving advances in malaria drug discovery. Through careful experimental design, analytical rigor, and collaborative teamwork, researchers can address complex biological challenges and contribute to global health solutions.<blockquote>This text has been automatically transcribed from a video presentation using AI technology. It may contain inaccuracies and is not guaranteed to be 100% correct.</blockquote><blockquote><h4>Concentrating on Chromatography Podcast</h4>Dive into the frontiers of chromatography, mass spectrometry, and sample preparation with host David Oliva. Each episode features candid conversations with leading researchers, industry innovators, and passionate scientists who are shaping the future of analytical chemistry. From decoding PFAS detection challenges to exploring the latest in AI-assisted liquid chromatography, this show uncovers practical workflows, sustainability breakthroughs, and the real-world impact of separation science. Whether you’re a chromatographer, lab professional, or researcher you'll discover inspiring content!You can find Concentrating on Chromatography Podcast in podcast apps:<ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL">Spotify</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185">Apple podcast</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography">podscan</a></li></ul>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos">YouTube channel</a></blockquote>

Affinity, Gel Filtration, Size Exclusion Chromatography: Repurposing Kinase Inhibitors for Malaria

In the week of February 9, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.<blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars">👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</a></h4>👉 Search and filter in the largest global database with over 5 000 GC, LC, MS and spectroscopy webinars.</blockquote><h5>1. SelectScience: High-Throughput Stability Screening Strategies for Antibody Formulation</h5><ul><li>Tu, 10.2.2026 17:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5807">Registration</a></li></ul>Learn how high-throughput DLS/SLS and rapid-screening DSC accelerate stability assessment of high-concentration antibody formulations, enabling faster, data-driven biologics development.<h5>2. Phenomenex: Big Scale, Big Wins – Prep Chromatography Explained</h5><ul><li>We, 11.2.2026 10:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5793">Registration</a></li></ul>Learn how to scale analytical methods to preparative HPLC, optimize loading capacity, and understand the limits of preparative columns for pharmaceutical applications.<h5>3. ALS Czech Republic: PFAS in Food &amp; Food Contact Material</h5><ul><li>We, 11.2.2026 15:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5816">Registration</a></li></ul>Get a practical overview of PFAS in food and food contact materials, including EU and US regulations, key analytical challenges, and reliable PFAS testing strategies.<h5>4. New Food Magazine: The Science of Next-Gen Ingredients – Fermentation, Formulation and Function</h5><ul><li>We, 11.2.2026 16:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5720">Registration</a></li></ul>Explore how fermentation-driven innovation is transforming functional food ingredients and how advanced analytics optimize flavour, functionality, and stability.<h5>5. SCIEX: Accurate Mass Fundamentals – Interpreting and Applying Your Data</h5><ul><li>We, 11.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5772">Registration</a></li></ul>Session 3 focuses on interpreting and applying accurate mass data to confirm compound identity, move beyond basic quantitation, and troubleshoot results for confident reporting.<h5>6. Agilent Technologies: Process Analytical Techniques – Online HPLC for Real-Time Monitoring and Control of Bioprocesses</h5><ul><li>Th, 12.2.2026 06:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5834">Registration</a></li></ul>Discover how PAT HPLC enables near-real-time monitoring of critical quality attributes in bioprocessing, with a case study on charge-variant control by cation-exchange chromatography.<h5>7. Thermo Fisher Scientific: Introducing the Orbitrap Excedion Pro Hybrid MS</h5><ul><li>Th, 12.2.2026 11:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5889">Registration</a></li></ul>Discover the new Orbitrap Exploris Pro with expanded ETD/EThcD capabilities for confident biopharmaceutical characterization, including intact proteins, PTMs, ADCs, and large biomolecules.<h5>8. Waters Corporation: Planning Your NuGenesis Upgrade – Insights and Best Practices for a Smooth Transition</h5><ul><li>Th, 12.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5833">Registration</a></li></ul>Learn how to plan a successful NuGenesis upgrade, transition to Windows 11, and unlock new capabilities such as dashboards for real-time operational insights.<h5>9. Thermo Fisher Scientific: Comprehensive Analytical Strategies for Peptide Therapeutics and GLP-1 Agonists with Agilent</h5><ul><li>Th, 12.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5814">Registration</a></li></ul>Explore analytical workflows for peptide therapeutics, including method development, peptide mapping, GLP-1 QC, and LC-MS strategies across Agilent platforms.<h5>10. Agilent Technologies: Moving from R&amp;D and Limited QC on a UV-Vis-NIR Instrument to Large-Scale QC Using an Autosampler</h5><ul><li>Th, 12.2.2026 20:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/2104">Registration</a></li></ul>This webinar covers practical aspects of adding and using an autosampler to maximize UV-Vis-NIR QC workflows at scale.<h5>11. Agilent Technologies: LC Method Transfer – Hidden Challenges &amp; Absolute Solution</h5><ul><li>Fr, 13.2.2026 06:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5787">Registration</a></li></ul>Discover why LC method transfer between legacy and modern systems is challenging, which hidden parameters affect retention and peak shape, and how to achieve robust, reliable results.

Webinars LabRulezLCMS Week 07/2026

Charge detection mass spectrometry (CDMS) allows direct mass determination of individual ions and is increasingly used to study heterogeneous biological samples. This work demonstrates the use of Orbitrap-based CDMS/Direct Mass Technology (DMT) for quantitative analysis of transthyretin (TTR) tetramer samples below 100 kDa, extending CDMS beyond its traditional qualitative role.DMT resolved wild-type and C-terminally modified TTR homotetramers, as well as hybrid tetramers, enabling kinetic analysis of subunit exchange and stability. The approach also quantified thyroxine binding to TTR variants, revealing differences in binding affinity linked to C-terminal modification. By separating overlapping m/z signals through charge measurement, CDMS enables accurate mass and abundance determination, highlighting its potential for quantitative analysis of complex protein systems.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771">Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology</a></h4>Robert L. Rider, Jared Hampton, Zhenyu Xi, Carter Lantz, Sangho D. Yun, Weijing Liu, Rosa Viner, Arthur Laganowsky, and David H. Russell*Anal. Chem. 2025, 97, 49, 27057–27063<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.analchem.5c05771">https://doi.org/10.1021/acs.analchem.5c05771</a><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.Transthyretin (TTR) is a homotetrameric transport protein that circulates in plasma and cerebrospinal fluid, delivering thyroxine (T4) and retinol-binding protein–vitamin A complexes. <a href="javascript:void(0);">(1)</a> The stability of the TTR tetramer is central to its physiological role because dissociation into monomers can initiate misfolding and amyloid formation, leading to systemic or hereditary transthyretin amyloidosis. <a href="javascript:void(0);">(2)</a> Subunit exchange between wild-type (WT) and variant TTR proteoforms, including disease-associated mutations such as V30M and V122I, have been implicated in amyloid progression by generating hybrid tetramers (tetramers containing WT and mutant subunits) with altered stabilities. <a href="javascript:void(0);">(3,4)</a> Ligand binding, particularly at the two thyroxine-binding sites located at the dimer–dimer interface, can kinetically stabilize the tetramer and modulate amyloidogenicity. <a href="javascript:void(0);">(5,6)</a> Accurate measurement of both subunit exchange kinetics and ligand binding stoichiometry is therefore critical for elucidating the TTR dynamics and stability.Affinity or sequence tags are widely employed in protein expression, purification, or detection. <a href="javascript:void(0);">(7,8)</a> While these tags are often assumed to be inert, their influence on protein structure and dynamics are rarely examined in detail. <a href="javascript:void(0);">(9,10)</a> Protein tags at the N- and C-terminus of TTR have been shown to have differing gas phase stabilities from those of WT-TTR. <a href="javascript:void(0);">(11)</a> The C-terminus is of particular interest because this region participates in the dimer–dimer interface that governs tetramer stability. <a href="javascript:void(0);">(11,12)</a> Characterizing how the C-terminal tag (CT) (-ASGENLFYQ) affects TTR’s solution stability and ligand binding is not only relevant for understanding TTR dynamics but also provides an example of how expression tags can alter protein dynamics. <a href="javascript:void(0);">(13)</a>Native mass spectrometry (nMS) has been invaluable for characterizing protein complexes, <a href="javascript:void(0);">(14)</a> yet conventional nMS often struggles with heterogeneous samples where overlapping charge state distributions and adduct heterogeneity limit resolution and quantitation. <a href="javascript:void(0);">(15)</a> Charge detection mass spectrometry (CDMS) addresses these limitations by independently measuring the charge and m/z of individual ions, enabling the direct determination of molecular mass and abundance. Development of CDMS has largely focused on achieving higher mass resolution <a href="javascript:void(0);">(16)</a> and extending measurements toward assemblies into the GDa range. <a href="javascript:void(0);">(17,18)</a> However, there is untapped utility for CDMS experiments other than mass and proteoform determination. Jordan et al. showed the capability to assess conformational heterogeneity of mAb aggregates using the added charge dimension that CDMS provides. <a href="javascript:void(0);">(19)</a> The current work demonstrates that CDMS can separate proteoforms with overlapping m/z values based on charge and quantify their relative abundances in complex mixtures. While nMS is already a highly quantitative technique, our results establish CDMS as an equally powerful tool for quantitative analysis in heterogeneous systems. <a href="javascript:void(0);">(20,21)</a>Here, we apply Orbitrap-based CDMS/Direct Mass Technology (DMT) using the selective temporal overview of resonant ions (STORI) approach <a href="javascript:void(0);">(22,23)</a> to quantitatively compare WT-TTR and CT-TTR, focusing on two biologically relevant properties: tetramer stability assessed via subunit exchange kinetics and ligand-binding affinity. Conventional nMS cannot fully resolve the overlapping charge states of WT- and CT-TTR or their ligand-bound states. However, DMT can resolve these species by directly measuring the mass (m/z × charge), enabling quantitation of all proteoforms. The data reveal that the CT tag alters tetramer stability and thyroxine-binding affinity, demonstrating the structural sensitivity of TTR to modifications at its C-terminus. More broadly, this work demonstrates the impact that protein tags can have on native protein interactions and highlights the broader utility of quantitative CDMS for probing heterogeneous biological samples.<h4>Experimental Section</h4><h5>Data Collection</h5>All experiments were conducted on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/560">Thermo Scientific Q-Exactive UHMR</a> with added DMT capabilities (Bremen, Germany). Before DMT, mass spectra were collected at various resolving powers (6–200k) for each sample, with the instrument parameters reported in the Supporting Information (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Table S1</a>). For DMT experiments, the trapping gas pressure in the HCD cell was reduced to 0.3–0.8 to attenuate the signal intensity to a single ion level, as well as decreasing the UHV pressure to assist ion retention through the entire transient of Orbitrap analysis. We observed no significant difference between mass spectra collected at various HCD cell pressures (Supporting Information, <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S1</a>). For DMT collection, automated ion control (AIC) and 100% target density were used with 200k resolving power.<h4>Results and Discussion</h4>CDMS has emerged as a powerful tool for analyzing heterogeneous biomolecular samples, enabling accurate, direct mass determination by simultaneously measuring the charge and m/z for individual ions. While CDMS has been widely applied for qualitative analyses, its potential for quantitative and less than MDa applications remains underexplored. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>A shows the theoretical mass spectrum of WT-TTR (14+ to 16+) and CT-TTR (15+ to 17+) homotetramers, where the two proteoforms become increasingly resolved as the charge states increase (&lt;3900 m/z). <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>B zooms in on the 14+ (WT) and 15+ (CT) charge states, highlighting their strong overlap, which prevents accurate deconvolution of the proteoforms by conventional methods. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>C displays theoretical distributions for 0, 1, and 2 T4 bound states of both WT- and CT-TTR tetramers, where &lt;3900 m/z has observable separation between all proteoforms. However, for the 14+ and 15+ charge states of WT- and CT-TTR, respectively, the 0 T4- and 1 T4-bound populations overlap (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>D). Furthermore, commonly adducted species (Na+, K+, and Zn2+) observed in experimental spectra broaden these distributions, making it increasingly difficult to distinguish and deconvolute the proteoforms (see <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S2</a>). Here, we employ Orbitrap-based CDMS/DMT to overcome this m/z overlap to resolve and quantify hybrid tetramer formation and T4 binding.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 1. (A) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers. (B) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions to show the large overlap of the proteoforms. (C) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine (T4) binding. (D) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions where the 0 and 1 T4 have overlapping distributions. These theoretical distributions do not contain any commonly adducted species (Na+, K+, Zn2+), which broaden the distributions and create more overlap even for the proteoforms in the range 3300–3900 m/z (see Figure S2)." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg 187w," sizes="100vw" width="1417" height="1182"><h5>Thyroxine Binding to TTR Homotetramers</h5>Thyroxine is the less active form of a thyroid hormone important for metabolism that binds to TTR for transport throughout plasma and cerebral spinal fluid. <a href="javascript:void(0);">(31)</a> Turnover of T4 into T3 (active) occurs after dissociation, where it can then modulate gene expression via binding to nuclear receptors. <a href="javascript:void(0);">(32)</a> The TTR tetramer gains substantial stability as it binds up to 2 T4 at the tetramer interface, decreasing tetramer dissociation and SUE. <a href="javascript:void(0);">(33)</a> This has been shown previously to decrease the amyloidogenic rate of TTR, which led to tafamidis (similar in structure to T4) to be designed and is currently the only drug that is approved for clinical treatment of TTR amyloidosis. <a href="javascript:void(0);">(34)</a> Measuring the difference in binding affinity between TTR proteoforms may provide insight into regions of TTR or TTR intermolecular/intramolecular interactions that are important for binding of small molecules such as tafamidis and T4.DMT was further applied to quantify T4 binding to WT- and CT-TTR homotetramers, highlighting the technique’s utility in probing protein–ligand interactions. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>A shows a representative mass spectrum of TTR homotetramers in the presence of T4. While ligand-bound species can be observed, homotetramers cannot be confidently resolved across the entire 3000–5000 m/z range. By leveraging the charge-resolving capabilities of DMT, we achieve separation of the homotetramers (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>B,C) and the 0, 1, and 2 ligand-bound states. The 2D plot clearly shows the gain in resolution achieved when charge is simultaneously measured with m/z by separating the 14+ and 15+ charge states for WT and CT, respectively, in the range 3900–4200 m/z. Additionally, using ion mobility does not provide the same kind of 2D resolution due to the similarity in arrival times for the homotetramer proteoforms, as evidenced by <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figures S4 and S5</a> (see the Supporting Information). These data provide evidence that when ion mobility is able to separate out species that overlap in m/z yet differ in mobility, CDMS could be an alternative or used complementarily since the species likely also differ in charge.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 3. (A) Mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine binding. Ligand binding can be resolved, but homotetramers cannot be confidently identified. Charge states labeled are for WT; CT is always one charge state higher at the same m/z range. (B) DMT heatmap resolving WT-TTR and CT-TTR homotetramers with the additional measurement of charge. (C) Deconvoluted mass spectrum from DMT analysis. Both homotetramers and their ligand binding are resolved, and fit for analysis is shown in red. (D) Mole fraction of each homotetramer and their thyroxine binding species. Error bars represent the standard deviation of replicates (n = 3). The significance for each ligand state is in respect to the left adjacent state. *p &lt; 0.05." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg 181w," sizes="100vw" width="1266" height="1094"><h4>Conclusion</h4>This work demonstrates that quantitatively, Orbitrap-based CDMS/DMT can determine differences in protein-complex stability and ligand binding. By directly comparing WT- with CT-TTR, we show that the CT tag accelerates tetramer dissociation while enhancing T4 binding affinity. These results indicate that the C-terminus, located at the dimer–dimer interface, plays a more significant role in TTR stability and ligand recognition than previously appreciated. <a href="javascript:void(0);">(12)</a> Even the addition of a short peptide sequence perturbs noncovalent interactions at the interface, likely altering solvent accessibility, and the dynamics of the thyroxine binding channel. <a href="javascript:void(0);">(37,54)</a> Such findings underscore the importance of evaluating how seemingly minor sequence modifications, such as affinity tags, can influence fundamental biophysical properties.Beyond TTR, this work positions quantitative CDMS as a broadly applicable strategy for analyzing heterogeneous protein systems, where charge domain separation overcomes the resolution limits of m/z domain measurements in traditional nMS experiments. While much of the field has emphasized extending CDMS to ultrahigh masses and maximal resolution, <a href="javascript:void(0);">(16,18)</a> our results highlight the underexplored potential of applying the method in the 1000–10,000 m/z range common to nMS experiments. This capability is directly relevant to heterogeneous membrane protein complexes, which often display broad distributions of oligomeric states, PTMs, lipid, and ligand adducts that complicate spectra. <a href="javascript:void(0);">(48,55)</a> Similarly, mAbs can oligomerize and exhibit mass heterogeneity from variable glycosylation, affecting pharmacokinetics, effector function, and stability. <a href="javascript:void(0);">(19)</a> CDMS may resolve and quantify such proteoforms in a single experiment without the need for charge reduction or chemical derivatization. <a href="javascript:void(0);">(48,56,57)</a>

Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology

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Organomation, founded in 1959, designs and manufactures high-quality nitrogen evaporators and extraction systems. Known for innovation and durability, their lab instruments are used globally for efficient sample preparation with strong customer support.

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Waters Corporation

This time we will give an overview and demonstration of the SELECT SERIES MRT for small molecule metabolite workflows such as metabolomics and drug metabolite identification.
During this demo, Adam will show how the MRT’s mass resolution of 200,000 and sub ppm mass accuracy for MS and MS/MS data can be maintained at the fast acquisition rates needed for integration with UPLC and how this aids metabolite identification. In addition, you will discover new acquisition modes which further enhance performance.
The session will conclude with a live Q&amp;A where Adam and other members of the team will be on hand to answer all of your questions. 
Why Should You Attend?
<ul>
<li>Discover how the characteristics of the MRT combine with UPLC to aid metabolic profiling workflows.</li>
<li>Learn how the different acquisition modes work to enhance performance.</li>
<li>Understand how MRT data is processed for various small molecule workflows.</li>
</ul>
<blockquote>
Presenter: Adam King (Senior Scientist, MS Discovery Program, Waters Corporation)
</blockquote>
<blockquote>
Adam joined Waters in 2015 working for the phenotyping group based at Imperial College London, supporting the National Phenome centre with technical support and training. In 2018, Adam relocated to Wilmslow as part of the biomedical research team within SciOps focusing on metabolomic analysis using Waters high resolution MS solutions and Ion mobility.
</blockquote>
<blockquote>
Prior to joining Waters, Adam obtained his BSc in Biochemistry from Kingston University, London, and worked in the pharmaceutical industry leading a team of scientist analyzing NCEs by LC-MS in the company&#39;s bioanalytical team.
</blockquote>
<blockquote>
Currently Adam is a Senior Scientist in the MS Discovery program group continuing to focus on high resolution MS and IM for metabolomics. Additionally, Adam is in the final stages of completing a part-time PhD in Metabolomics at Murdoch University in Perth, Australia.
</blockquote>

Unquestioned Confidence in Metabolic Profiling

How the MRT’s mass resolution of 200,000 and sub ppm mass accuracy for MS and MS/MS data can be maintained at the fast acquisition rates.

In our third SELECT SERIES MRT in Action deminar join us to see how the exceptional resolving power of the MRT can help you make faster and better-informed decisions on Biopharmaceutical workflows.
During the demo, Dale will show how subtle modifications to primary structure such as differences to the isotope distributions of native and deamidated peptides can be unveiled with the MRT and how the high resolution of the MRT has benefits for protein analysis in that fully-resolved isotope distributions can be obtained, aiding in deconvolution to monoisotopic mass.
The session will conclude with a live Q&amp;A where Dale and other members of the team will be on hand to answer all of your questions. 
Why Should You Attend?
<ul>
<li>Discover how the characteristics of the MRT aid biologics characterization workflows.</li>
<li>Learn how the different acquisition modes work to enhance performance.</li>
<li>Understand how MRT data is processed for various biopharmaceutical workflows.</li>
</ul>
<blockquote>
Presenter: Dale Cooper-Shepherd (Principal Scientist, Advanced Mass Spectrometry, Waters Corporation)
</blockquote>
<blockquote>
Dale is a Senior Scientist in the Discovery MS group at Waters, Wilmslow, UK. He undertook PhD studies at the University of Leeds and conducted postdoctoral research at the University of Oxford, UK. Throughout his training Dale specialized in applying ion mobility MS in the field of structural biology.
</blockquote>
<blockquote>
Dale joined Waters in 2015 and since 2019 has been working as an applications scientist on the SELECT SERIES of instruments.
</blockquote>

Elevated Biologics Characterization

How subtle modifications to primary structure such as differences to the isotope distributions of native and deamidated peptides can be unveiled with the MRT.

Glycoproteins are gaining special recognition in proteomics thanks to their multiple roles in biological processes, be it as biopharmaceuticals or as disease biomarkers in pathological processes.
The bottom-up analysis of glycopeptides therefore offers important advantages for glycoprotein characterization, providing information about the structure and composition of the glycans and about the carrier protein.
In this webinar, our expert speakers will discuss how to optimize glycopeptide analysis using capillary liquid chromatography coupled to tandem mass spectrometry, showcasing how the ZenoTOF 7600 system enhances the analysis of proteins and their post-translational modifications.
Attend this webinar to: 
<ul>
<li>Learn how to design an LC-MS/MS experiment that optimizes acquisition parameters for glycan analysis
</li>
<li>Discover the importance of all steps in the workflow, including peak picking and search parameters during data processing
</li>
<li>Explore how improved parameters boost the annotation of glycopeptides
</li>
</ul>
<blockquote>
Presenter: Dr. Estela Giménez (Associate Professor, University of Barcelona)
</blockquote>
<blockquote>
Presenter: Dr. Maarten Dhaenens (Executive PI ProGenTomics, Ghent University)
</blockquote>

Technology Networks: Improving Peptide Annotation and Glycan Localization Using EAD 

Improving Peptide Annotation and Glycan Localization Using EAD 

How to optimize glycopeptide analysis using capillary liquid chromatography coupled to tandem mass spectrometry.

Improving Peptide Annotation and Glycan Localization

Host-associated microbial communities are unique sources for natural product drug discovery.
By studying these microbes, novel and targeted drug leads can be identified and critical questions answered within the broader field of chemical ecology.
Dr. Balunas’ research connects the dots between microbes, metals and metabolites to discover new medicines for a wide range of human diseases.
In this webinar, Dr. Balunas will showcase her latest research into deriving natural products from the marine invertebrate Botryllus schlosseri.
Attend this webinar to discover:
<ul>
<li>Marine natural product drug discovery
</li>
<li>Advanced informatics tools for metabolomics
</li>
<li>Untargeted metabolomics with timsTOF
</li>
</ul>
<blockquote>
Presenter: Dr. Marcy Balunas (Associate Professor, University of Michigan)
</blockquote>

Technology Networks: Dive Into Microbes, Metals and Metabolites for Drug Discovery

Dive Into Microbes, Metals and Metabolites for Drug Discovery

Latest research into deriving natural products from the marine invertebrate Botryllus schlosseri.

Microbes, Metals and Metabolites for Drug Discovery

The identification of extractables, leachables and chemical migration is a challenge for manufacturers and suppliers of packaging materials, medical devices and food contact materials. E&amp;L analytics is already complex, but it is compounded by legislative and regulatory efforts to recycle plastics. Analytical methods need to screen for not only the known components but also identify degradants and other unexpected compounds. Manufacturers, producers and retailers face the challenge of keeping up with evolving requirements and developing and adapting strategies to reduce plastic waste.
Thus, ways are being explored to incorporate more recycled plastics into products and packaging while maintaining excellent safety, quality and performance characteristics. As they innovate and combine new materials, companies must demonstrate safety and confirm compliance before bringing their products to market. This again increases the demand and importance of highly effective analytics.
Register now for this virtual event and share knowledge and challenges with peers and E&amp;L experts.
Who Should Attend?
The webinars are focused on the needs of scientists working in the area of Extractables &amp; Leachables and Food Contact Materials. During these webinars, attendees will learn:
<ul>
<li>Upcoming and new regulations in the field of food, pharma, biopharma and medical devices
</li>
<li>Targeted and non-targeted screening workflows by using Waters_Connect
</li>
<li>Characterization and structural elucidation of unknowns
</li>
<li>Choice of chromatographic techniques, extraction methods and analytical standards &amp; reagents
</li>
</ul>
<h3>EPISODE 3 - Virtual European Workshop on Extractables &amp; Leachables for Medical Devices</h3>
Agenda:
<h4>The role of chemical characterization in the evaluation of the biological safety of medical devices</h4>
<ul>
<li>Dr. Séverine Colas, Chief Scientific Officer, TentaConsult Pharma &amp; Med GmbH, Germany</li>
</ul>
<h4>Chemical Characterisation of Dressings: Extraction and Analytical Challenges</h4>
<ul>
<li>Pauline Kisseleff, Analytical Expert, URGO Recherche Innovation et Développement, France</li>
</ul>
<h4>Leachables from Pharma and Medical device materials, a non-target challenging analysis</h4>
<ul>
<li>Prof. Cristina Nerin, University of Zaragossa, Spain</li>
</ul>
<blockquote>
Presenter: Dr. Séverine Colas (Chief Scientific Officer, TentaConsult Pharma &amp; Med GmbH)
</blockquote>
<blockquote>
Séverine Colas is a PhD and a toxicologist (ERT) with more than fifteen years of experience in regulatory toxicology. She has always worked in services for the safety and regulatory compliance of products, initially with pharmaceuticals, then with chemicals and for more than 10 years now with medical devices. She has joined the TentaConsult team to provide to the client her strong expertise on biological evaluation of medical devices (MDR, ISO 10993-1 and related guidelines) and support them to establish the best strategy for the compliance of their medical device throughout their life cycle. If testing is needed to complete the evaluation, she also provides the client with her experience in conducting biocompatibility studies to find the suitable laboratory and to establish the more pertinent study design. As Chief Scientific Officer and Sales Director in TentaConsult, she is the preferred contact of the client to provide the best offer for the need.
</blockquote>
<blockquote>
Presenter: Pauline Kisseleff (Analytical Expert, URGO Recherche Innovation et Développement)
</blockquote>
<blockquote>
Pauline Kisseleff has a Master degree in analytical chemistry and received her PhD on container-content interactions applied to cosmetic products in 2020. She is currently in charge of extractables and leachables studies at URGO Research, Innovation and Development, where she works on several medical devices such as technological dressings
</blockquote>
<blockquote>
Presenter: Cristina Nerin (Professor, Department of Analytical Chemistry, University of Zaragoza)
</blockquote>
<blockquote>
Full Professor at the University of Zaragoza (Spain), PhD in Analytical Chemistry, Master in Science (Analytical Chemistry) and Degree in Chemistry at the University of Zaragoza (Spain). Director of the Research Group GUIA at the University of Zaragoza and Director of the Master in Environmental Engineering at the University of Zaragoza from 1990 to 2012. Author of more than 395 Scientific Publications included in the Citation Index, Director of 38 PhD Thesis (5 more are in process). Principal Investigator of more than 240 Research Projects in both Competitive calls and also R&amp;D&amp;I with Industry Inventor in six International Patents dealing with active packaging and in one International Patent on Intelligent Packaging. All of them are in exploitation (market). Six Research Awards received. Participant in more than 140 International Conferences and Professor of several International Courses n Europe, Asia and South-America.
</blockquote>

Waters Corporation: Virtual European Workshop on Extractables & Leachables for Medical Devices

Virtual European Workshop on Extractables & Leachables for Medical Devices

Register now for this virtual event and share knowledge and challenges with peers and E&L experts.

Virtual European Workshop on Extractables & Leachables

The advancement of CRISPR-based gene editing tools into biotherapeutics offers the potential for cures to genetic disorders and for new treatment paradigms for even common diseases.
Arguably, the most important component of a CRISPR-based medicine is the guide RNA that dictates the on-target editing site as well as potential undesired off-target edits.
To ensure the spacer region is of high fidelity, top-down mass spectrometry was implemented to provide direct and quantitative assessments of highly modified gRNA. In addition to sequencing the spacer region and pinpointing modifications, top-down mass spectra were utilized to quantify single-base spacer substitution impurities down to &lt;1% and to decipher highly dissimilar spacers. 
To accomplish these results in an automated fashion, we devised custom software capable of sequencing and quantifying impurities in gRNA spacers. Notably, we developed automated tools that enabled the quantification of single-base substitutions, including advanced isotopic pattern matching for C &gt; U and U &gt; C substitutions, and created a de novo sequencing strategy to facilitate the identification and quantification of gRNA impurities with highly dissimilar spacer regions.
By attending this presentation you will:
<ul>
<li>Gain an understanding of gRNA spacer characterization by MS/MS.
</li>
<li>Learn about gRNA impurity analysis by MS/MS.
</li>
</ul>
<blockquote>
Presenter: Luis A. Macias, PhD (Mass Spectrometry Scientist, Verve Therapeutics)
</blockquote>
<blockquote>
Luis joined Verve in 2022 as a mass spectrometry scientist focusing on support and development of gRNA characterization methods. Prior to joining Verve, Luis was a graduate student in the Brodbelt lab at the University of Texas, where he developed mass spectrometry-based methods to examine structural features of proteins and lipids.
</blockquote>

Separation Science: Spacer Fidelity Assessments of Guide RNA by Top-Down Mass Spectrometry

Spacer Fidelity Assessments of Guide RNA by Top-Down Mass Spectrometry

Learn about gRNA impurity analysis by MS/MS.

Spacer Fidelity Assessments of Guide RNA

Ion Mobility (IM) advancements in Software, Data Bases, AI and Machine learning are quickly improving capabilities to make unknown identifications, separate and ID isomers, as well as improve workflows associated with metabolomics, lipidomics, PFAS, and qual-quant screening.
In addition, IM measurements are significantly improved with HRdm High Resolution Demultiplexing. This is the first commercial IM instrument to enable the simultaneous combination of high drift resolution, while at the same time achieving all four of the following measurement capabilities: broad mass range in a single injection, multiplexing to increase sensitivity, compatibility with fast chromatographic acquisition rates , and highest precision in CCS measurements. For more accurate CCS predictions, the better precision in the CCS training set improves AI machine learning SW. This can significantly reduce the number of potential candidate structures to select from when making unknown identifications.
<blockquote>
Presenter: Xueyun Zheng, PhD (Integrative Omics Group, Pacific Northwest National Laboratory)
</blockquote>

Agilent Technologies: LipidOz: an Open-source Tool for Automated Elucidation of Lipid Double Bond Positions from Ozone-Induced Dissociation-IMS-MS Data

LipidOz: an Open-source Tool for Automated Elucidation of Lipid Double Bond Positions from Ozone-Induced Dissociation-IMS-MS Data

LipidOz: an Open-source Tool for Automated Elucidation of Lipid Double Bond Positions from Ozone-Induced Dissociation-IMS-MS Data.

LipidOz: Elucidation of Lipid Double Bond Positions IMS-MS

Ion Mobility (IM) advancements in Software, Data Bases, AI and Machine learning are quickly improving capabilities to make unknown identifications, separate and ID isomers, as well as improve workflows associated with metabolomics, lipidomics, PFAS, and qual-quant screening.
In addition, IM measurements are significantly improved with HRdm High Resolution Demultiplexing. This is the first commercial IM instrument to enable the simultaneous combination of high drift resolution, while at the same time achieving all four of the following measurement capabilities: broad mass range in a single injection, multiplexing to increase sensitivity, compatibility with fast chromatographic acquisition rates , and highest precision in CCS measurements. For more accurate CCS predictions, the better precision in the CCS training set improves AI machine learning SW. This can significantly reduce the number of potential candidate structures to select from when making unknown identifications.
<blockquote>
Presenter: James Dodds, PhD (University of North Carolina)
</blockquote>

Agilent Technologies: Innovative Data Analysis Strategies for Advancing Ion Mobility MS Workflows featuring Skyline, HRdm High Resolution Demultiplexing, and MetaboAnalyst

Innovative Data Analysis Strategies for Advancing Ion Mobility MS Workflows featuring Skyline, HRdm High Resolution Demultiplexing, and MetaboAnalyst

Innovative Data Analysis Strategies for Advancing Ion Mobility MS Workflows featuring Skyline, HRdm High Resolution Demultiplexing, and MetaboAnalyst.

Strategies for Advancing Ion Mobility MS Workflows

Ion Mobility (IM) advancements in Software, Data Bases, AI and Machine learning are quickly improving capabilities to make unknown identifications, separate and ID isomers, as well as improve workflows associated with metabolomics, lipidomics, PFAS, and qual-quant screening.
In addition, IM measurements are significantly improved with HRdm High Resolution Demultiplexing. This is the first commercial IM instrument to enable the simultaneous combination of high drift resolution, while at the same time achieving all four of the following measurement capabilities: broad mass range in a single injection, multiplexing to increase sensitivity, compatibility with fast chromatographic acquisition rates , and highest precision in CCS measurements. For more accurate CCS predictions, the better precision in the CCS training set improves AI machine learning SW. This can significantly reduce the number of potential candidate structures to select from when making unknown identifications.
<blockquote>
Presenter: Amber Jones (MOBILion Corporation)
</blockquote>

Agilent Technologies: Tackling the Peptide Isomer Impurity Challenge with High-Resolution Ion Mobility Mass Spectrometry

Tackling the Peptide Isomer Impurity Challenge with High-Resolution Ion Mobility Mass Spectrometry

Tackling the Peptide Isomer Impurity Challenge with High-Resolution Ion Mobility Mass Spectrometry.

Peptide Isomer Impurity Challenge IMS-HRMS

Many labs are faced with an ever-increasing sample load and changing regulations, plus the need to analyze increasingly complex data, while instrumentation and resources remain at a steady level.
As a consequence, instrument throughput and uptime are critical factors to maintain competitiveness and productivity. You need instruments that have evolved into complete solutions for meeting your current and future challenges.
You can meet your challenges with the new Agilent Revident quadrupole time-of-flight LC/MS system (LC/Q-TOF) and Agilent 6495 triple quadrupole LC/MS (LC/TQ). Their easy-to-use onboard intelligence, harmonized operation, and complete workflow capabilities let you look beyond instrumentation and expand your lab’s potential. So, you can focus on what inspires you and meet every challenge that comes your way.
What&#39;s in it for you?
<ul>
<li>Discover Next-Gen Instruments: Witness the intelligent Agilent Revident quadrupole time-of-flight LC/MS system (LC/Q-TOF) and the Agilent 6495 triple quadrupole LC/MS (LC/TQ). These are more than instruments – they&#39;re your keys to unmatched data precision and analysis.
</li>
<li>Elevate Your Lab&#39;s Potential: Say goodbye to outdated methods and welcome complete intelligent workflows. Picture a lab where time-consuming tasks are streamlined, complex data analysis becomes seamless, and your team can focus on what truly matters.
</li>
<li>Ignite Your Curiosity: Curious minds create transformative science. Learn from industry experts as they dive deep into the realm of instrument intelligence, AI-based tuning, and instrument telemetry. Gain insights into how you can maximize efficiency and enhance the capabilities of your lab.
</li>
</ul>
Who Should Attend? 
<ul>
<li>Lab Managers: Lead your lab into a new era of efficiency and productivity.
</li>
<li>Principle Investigators: Fuel your research with cutting-edge technology and insights.
</li>
<li>Senior Scientists: Stay ahead of the curve by harnessing the power of intelligent instrumentation.
</li>
</ul>

Agilent Technologies: LCMS Intelligence Unveiled - Shaping Futuristic Labs

LCMS Intelligence Unveiled - Shaping Futuristic Labs

Agilent Revident quadrupole time-of-flight LC/MS system (LC/Q-TOF) and Agilent 6495 triple quadrupole LC/MS (LC/TQ).

LCMS webinars focusing on LC/TOF - page 22