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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Everything from the world of analytical chemistry in one place. We connect people in solving their problems. At Labrulez you will find all the necessary information easily, quickly and clearly. Stop searching and start finding.

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Agilent Technologies

Thermo Fisher Scientific

Shimadzu Corporation

SCIEX

Waters Corporation

Get insight into topics ranging from the history of PFAS to analytical testing methods.
Day 1: Participate in an open discussion forum with our internal PFAS scientists from across the globe. Hear the story of how PFAS has shaped our environmental research. Take advantage of this digital space to share, learn and teach your fellow colleagues in the PFAS testing world.
Join this event to:
<ul>
<li>Learn about the history of PFAS and the need to increase testing for these “forever chemicals”</li>
<li>Understand how PFAS regulations differ across the globe</li>
<li>See what the future could look like in the PFAS testing world</li>
<li>Explore different matrices for PFAS testing</li>
<li>Discover how LC-MS can help solve challenges related to testing for PFAS chemicals</li>
<li>Get tips and tricks from seasoned PFAS testing experts</li>
<li>Find out what your peers are doing and share your knowledge in our open forum</li>
</ul>
This 2-day event is the first session of many PFAS summits SCIEX will host in the coming year, and there will be exciting activities for you to participate in throughout 2023. Join us for this first session and find out more about the next one: the in-person version!
<h3>Agenda Day 1</h3>
<h5>A brief history of PFAS</h5>
<ul>
<li>Dr. Craig Butt (Manager, Applied Market, SCIEX)</li>
</ul>
<h5>Part 1: PFAS workflow overview: past, present and future</h5>
<h5>Part 2: The EMEAI perspective</h5>
<ul>
<li>Simon Roberts (Staff Application Scientist, SCIEX)</li>
<li>Jianru Stahl-Zeng (Senior Technical Manager, EMEAI, SCIEX)</li>
</ul>
<h5>PHX complementary workflow</h5>
<ul>
<li>Sam Lodge (Senior Business Development Manager, Phenomenex)</li>
</ul>
<h5>Automating the Solid Phase Extraction (SPE) of PFAS for a range of methods and matrices</h5>
<ul>
<li>Ian Wan (Product Manager, PromoChrom Technologies)</li>
</ul>
<h5>What does 4ppq actually look like?</h5>
<ul>
<li>Karl Oetjen (Senior Scientist, Technical Marketing, SCIEX)</li>
</ul>
<h5>PFAS and customer support overview</h5>
<ul>
<li>Megumi Shimizu (LC-MS Application Scientist, SCIEX)</li>
</ul>
<h5>An overview of different PFAS exposure pathways</h5>
<ul>
<li>Holly Lee (Food LC-MS Scientist, SCIEX)</li>
</ul>

PFAS summit: a scientific series (Day 1)

Join the discussion as SCIEX customers and industry experts explore how forever chemicals have shaped our environmental research.

Get insight into topics ranging from the history of PFAS to analytical testing methods.
Day 1: Participate in an open discussion forum with our internal PFAS scientists from across the globe. Hear the story of how PFAS has shaped our environmental research. Take advantage of this digital space to share, learn and teach your fellow colleagues in the PFAS testing world.
Join this event to:
<ul>
<li>Learn about the history of PFAS and the need to increase testing for these “forever chemicals”</li>
<li>Understand how PFAS regulations differ across the globe</li>
<li>See what the future could look like in the PFAS testing world</li>
<li>Explore different matrices for PFAS testing</li>
<li>Discover how LC-MS can help solve challenges related to testing for PFAS chemicals</li>
<li>Get tips and tricks from seasoned PFAS testing experts</li>
<li>Find out what your peers are doing and share your knowledge in our open forum</li>
</ul>
This 2-day event is the first session of many PFAS summits SCIEX will host in the coming year, and there will be exciting activities for you to participate in throughout 2023. Join us for this first session and find out more about the next one: the in-person version!
<h3>Agenda Day 2</h3>
<h5>Advancing LC-MS analyses for characterizing human exposure to PFASs</h5>
<ul>
<li>Christopher Higgins, PhD (University Distinguished Professor, Colorado School of Mines)</li>
</ul>
<h5>The ever-changing landscape of the modern PFAS laboratory</h5>
<ul>
<li>Andrew Patterson (Technical Director, Eurofins Specialty Services)</li>
</ul>
<h5>Environmental fate and global distribution of PFAS</h5>
<ul>
<li>Cora Young (ssociate Professor and Guy Warwick Rogers Chair, York University)</li>
</ul>
<h5>Screening of PFAS in cosmetics and personal care products</h5>
<ul>
<li>Amy Rand (Assistant Professor, Charlton University)</li>
</ul>

PFAS summit: a scientific series (Day 2)

The drive for lower analyte detection limits, increased laboratory productivity, and concerns around gas chromatography carrier gas availability and costs push the need for innovation in gas chromatography (GC) coupled with mass spectrometry (MS) technology.
The next generation of GC-MS is already here! Atmospheric Pressure Gas Chromatography (APGC) technology offers laboratories a powerful alternative to Electron Ionization (EI) technology, enabling low limits of detection and confident compound identification and confirmation, while reducing laboratory costs, from reduced GC system maintenance and the ability to use nitrogen as an alternative carrier gas.
Agenda
<ul>
<li>Understanding the next generation GC-MS/MS requirement</li>
<li>Top 5 benefits of Atmospheric Pressure Gas Chromatography Technology</li>
<li>Applications for Food &amp; Environmental Testing</li>
<li>Hear from our Experts!</li>
</ul>
<blockquote>
Presenter: Wim Broer (Development and Science, Nofalab)
</blockquote>
<blockquote>
Presenter: Rhys Jones (Principal Consulting Scientist, Waters Corporation)
</blockquote>
<blockquote>
Rhys has worked for Waters in research and development for 20 years with a strong focus on gas chromatography mass spectrometry. ​The early part of his career was spent developing and supporting the AutoSpec magnetic sector instrument. ​One of his current responsibilities is the research, development and support of the atmospheric pressure gas chromatography (APGC) chemical ionization source, which has allowed the full range of Waters’ mass spectrometry techniques to be applied to GC analyses.
</blockquote>

Waters Corporation: Next Generation GC-MS/MS for Food and Environment Application

Next Generation GC-MS/MS for Food and Environment Application

The next generation of GC-MS! Atmospheric Pressure Gas Chromatography (APGC) technology offers laboratories a powerful alternative to Electron Ionization (EI).

Next Generation GC-MS/MS for Food and Environment Apps

Don’t miss this exclusive look into how Trilogy Analytical Laboratory, a high-throughput food and feed safety laboratory, relies on robust LC-MS/MS solutions to consistently test for mycotoxins across a multitude of commodities with speed and selectivity.
We’ll look at:
<ul>
<li>How molds and the mycotoxins end up in grain</li>
<li>Differences between testing grain and its byproducts</li>
<li>Improving predictions of mycotoxin occurrence</li>
<li>Delivering trustworthy results to your clients quickly</li>
</ul>
<blockquote>
Presenter: Julie Brunkhorst
</blockquote>
<blockquote>
Julie Brunkhorst has been with Trilogy since it opened in 1999 and is currently the Vice-President of the Technical Division. As an essential part of Trilogy’s growth and success, Julie oversees the daily operations of the laboratory and directs all R&amp;D activities. Her expertise in designing procedures customized for high throughput laboratories has enabled Trilogy to reduce run times, and in many cases, offering same-day turnaround. Julie holds a BAS in Chemistry from Maryville University.
</blockquote>
<blockquote>
Presenter: Carrie Maune
</blockquote>
<blockquote>
Carrie Maune is President and CEO of Trilogy Analytical Laboratory and is one of the original founders of the organization. Carrie has dedicated 23 years of her professional life to helping build Trilogy into the industry-trusted laboratory that it is today. Carrie has 35+ years of mycotoxin experience and has a passion for sharing her knowledge with others. Carrie is a graduate of Central Missouri University.
</blockquote>
<blockquote>
Presenter: Jordon Bierbaum
</blockquote>
<blockquote>
Jordon Bierbaum is the Vice-President of Operations at Trilogy Analytical Laboratory. Jordon started with the organization in 2009 as a chemist and quickly advanced within the laboratory. Jordon has held management positions within Trilogy’s laboratory and production department and this well-rounded experience give him a unique knowledge of quality processes and quality materials. Jordon has his BS of Science in Medicinal Chemistry from the University of Missouri-Columbia and an MBA from Missouri Baptist University.
</blockquote>

SCIEX: The truths, myths, and intricacies of testing mycotoxins

The truths, myths, and intricacies of testing mycotoxins

How Trilogy Analytical Laboratory relies on LC-MS/MS solutions to consistently test for mycotoxins across a multitude of commodities with speed and selectivity.

One declared goal of the EU is that all surface and groundwater bodies achieve good chemical and good ecological status. Pollutants of great concern are regulated within the Water Frame Work Directive 2000/60/EC, amongst them a number of pesticides. The so-called Surface Water Watch Lists help to identify and monitor new substances of concern. On these lists are more and more pharmaceuticals as well as personal care products.
For this reason we developed a multi-residue LC-MS/MS method with the aim to:
<ul>
<li>quantify more than 140 pesticides, pharmaceuticals and personal care products in one run and</li>
<li>reach LOQs of 10 ng/l for all compounds with direct injection of aqueous samples.</li>
</ul>
In this webinar Hannah Willmer will present:
<ul>
<li>What method conditions and instrumentation are needed?</li>
<li>Which are the most challenging compounds?</li>
<li>How does the new waters_connect for Quan software support method development?</li>
</ul>
<blockquote>
Presenter: Hannah Willmer (Senior Applications Chemist, Waters Corporation)
</blockquote>
<blockquote>
Hannah Willmer is an applications chemist in the European demo lab, based in Wilmslow, UK. Her main role focuses on application development work for the food and environmental sector.
</blockquote>
<blockquote>
With a background in bioanalysis supporting the pharmaceutical sector, Hannah further developed a passion for the food and environmental industry. She cultivated this enthusiasm in a contract organization for 6 years where she managed a team and developed methods for the analysis of food and supplements from nutritional testing to food safety compliance. She specialized within the pesticides and contaminants department with a focus on infant formula which brings its own challenges such as more stringent regulations and high throughput.
</blockquote>
<blockquote>
As a former research analyst and Waters client Hannah understands the importance of robust and reliable methods to Waters’ customers and strives to enhance the customers’ experience with the quality comprehensive solutions that are essential to meet the demands in modern testing.
</blockquote>

Waters Corporation: LC-MS/MS Multi-residue Method for Pesticides, Pharmaceuticals and Personal Care Products (PPPCPs) in Water

LC-MS/MS Multi-residue Method for Pesticides, Pharmaceuticals and Personal Care Products (PPPCPs) in Water

What method conditions and instrumentation are needed?; Which are the most challenging compounds?; How does the new waters_connect support method development?

LC-MS/MS Multi-residue Method for Water analysis

LC-MS/MS is rapidly becoming the gold standard for quantifying different classes of analytes in endocrinology research. The power of greater selectivity and analytical sensitivity using LC-MS/MS is critical in understanding the status of endocrine biochemical pathways. The enhanced performance observed on these platforms provides increased confidence in the results, enabling you to make better decisions based on more accurate information.
Greater analytical sensitivity is a goal that drives improvements in precision, leading to clearer insights into results down to low physiological concentrations. Here we will discuss the latest introduction to the Waters MassTrak™ IVD system family, which is shown to be analytically sensitive and efficient, helping to reduce cost and improve the quality of your data. 
Learning objectives: 
<ul>
<li>An introduction to the latest addition to Waters MassTrak IVD System for clinical laboratories
</li>
<li>The importance of selectivity in endocrinology research in obtaining high quality data
</li>
<li>How the latest addition to Waters MassTrak IVD System addresses the needs of those key endocrinology research applications, including steroid hormone analysis
</li>
</ul>
<blockquote>
Presenter: Dominic Foley (Principal Scientist, Waters Corporation)
</blockquote>
<blockquote>
Dominic is a Principal Scientist working at Waters Mass Spectrometry Headquarters in Wilmslow, UK. Having joined the company in September 2013, he has specialized in the development of LC-MS/MS clinical research applications, with expertise in steroid hormone analysis and protein/peptide quantification. In his role, he also collaborates with clinical customers in the development and implementation of LC-MS/MS methods in their laboratories.
</blockquote>
<blockquote>
Dominic has worked in separation sciences for 14 years, following his ambition of improving the quality of healthcare. He started his career with ICON Development Solutions, a CRO in the north of the UK, where he worked as a LC-MS/MS method development and validation scientist supporting DMPK studies in drug discovery. In 2012, he joined Thermo Fisher Scientific to work in their Chromatography R&amp;D team as a Technical Support Specialist, working on the development of new chromatography and sample preparation products.
</blockquote>
<blockquote>
Dominic received his BSc (Hons) in Biochemistry from the University of Manchester in 2006. He has presented his work at conferences around the world and has several publications in both the Microchemical Journal and the Journal of Chromatography A.
</blockquote>
<blockquote>
Presenter: David Ballantyne (Principal Product Manager, Waters Corporation)
</blockquote>
<blockquote>
David Ballantyne is a Principal Product Manager at Waters Corporation, working within the Global Clinical Diagnostics Portfolio Management team. Having joined the company in 2005, he has held multiple roles throughout Manufacturing and R&amp;D. David has a background in Electrical and Mechanical Engineering and began his career at Waters supporting GC-MS/MS technologies including Tandem Quadrupole and Magnetic Sector Mass Spectrometry.
</blockquote>
<blockquote>
In 2018 he moved to his role in Product Management where is focus changed to Clinical Diagnostics, with a particular focus on LC – MS/MS Instrumentation and Informatics solutions. Over the last 5 years David has spent much of his time focused on understanding customer problems and translating them into new solutions.
</blockquote>

Waters Corporation: The Evolving Power of LC-MS/MS Technology within Endocrinology

The Evolving Power of LC-MS/MS Technology within Endocrinology

Here we will discuss the latest introduction to the Waters MassTrak™ IVD system family for clinical laboratories.

The Evolving Power of LC-MS/MS within Endocrinology

This year we invite you to ignite your mind to Be Curious about what Ion chromatography (IC) can do with its versatility in many detections across the IC application spectrum to improve your workflows and solve challenges.
During this three day virtual event, learn from a panel of experts how the latest IC applications are helping colleagues achieve breakthroughs, and walk away with valuable information on how advancements in IC can increase laboratory analytical capabilities. 
Although each day is convenient for a specific region, you can attend any session on any day. All sessions and workshops will be available for on-demand viewing after the event concludes.
<h3>Day 3 Agenda | April 20 | Asia Pacific</h3>
Expand the world of electrochemistry applications and IC hyphenation with high-resolution mass spectrometry and understand how Inductively Coupled Plasma Spectrometry can speciate isotopes while simplifying Pharmacopeia QC analysis and keeping your IC in top-notch condition.
<h5>11:00 AM SGT: Opening Plenary: Electrochemical Detection and Its Application in Ion Chromatography</h5>
<ul>
<li>Yan Liu (Thermo Fisher Scientific, IC/SP R&amp;D, Sunnyvale)</li>
</ul>
<h5>12:00 PM SGT: Application of Anion Chromatography Coupled High-Resolution Mass Spectrometry to Increase Cellular Metabolite Coverage</h5>
<ul>
<li>Vinzenz Hofferek (McConville Lab, Department of Biochemistry and Pharmacology)</li>
</ul>
<h5>1:00 PM SGT: Analysis of Anhydrosugars and Xylooligosaccharides by Ion Chromatography with Electrospray Lithium Cationisation-Triple Quadrupole Tandem Mass Spectrometry</h5>
<ul>
<li>Dr. Estrella Sanz Rodriguez (Natural Products Analysis, Australian Centre for Research on Separation Science (ACROSS), University of Tasmania)</li>
</ul>
<h5>2:00 PM SGT: You Gotta Keep ‘Em Separated: Novel IC Applications for Subsequent Isotopic Analyses by Rapid and/or Hyphenated Techniques</h5>
<ul>
<li>Dr. Brandon Mahan (College of Science and Engineering, James Cook University)</li>
<li>Grace Manestar (IsoTropics PhD Candidate)</li>
</ul>
<h5>3:00 PM SGT: Use of Ion Chromatography in Pharmaceutical Quality Control</h5>
<ul>
<li>Catherine Frankis and Stella Planou (Reading Scientific Services Ltd., Reading Science Centre, Whiteknights Campus)</li>
</ul>
<h5>4:00 PM SGT: Tips on Keeping Your Ion Chromatography in Top-Notch Condition</h5>
<ul>
<li>Ryan Ong (Thermo Fisher Scientific, IC/SP Application Sales Support, Singapore)</li>
</ul>

Thermo Fisher Scientific: IC Symposium 2023

IC Symposium 2023 - Day 3

Join us for the 2023 Global IC Symposium! Day 3 | Asia Pacific.

<ul>
<li>Wait what?! Who knew!? There are so many things that a mass spec can do.
</li>
<li>I&#39;ve used it for years, yes this may be true.
</li>
<li>I&#39;ve processed some samples, more than a few.
</li>
<li>But between me and you, I had no idea all the things it could do!
</li>
<li>From sample prep to separation, you just won&#39;t believe…
</li>
<li>All of the tips and tricks we have up our sleeve.
</li>
<li>So, take a few minutes, about 15 should do.
</li>
<li>And learn all the things your mass spec can do.
</li>
</ul>
An easy to follow guide detailing how to set MS scan parameters for an LCMS experiment will be presented. Scan speeds for reproducible quantitation, chromatographic resolution, retention time definition, proper threshold adjustment for optimum datafile size, and how this can result in faster processing times will all be discussed.
<blockquote>
Presenter: Rebecca Glaskin, Ph.D. (LC/MS Application Scientist, Agilent Technologies, Inc.)
</blockquote>
<blockquote>
Rebecca Glaskin is an LC/MS Application Scientist at Agilent with a focus on BioPharma applications supporting the LC-Q/TOF and IM-QTOF platforms. Prior to joining Agilent, Rebecca received her Ph.D. in analytical chemistry from Indiana University in the lab of Professor David Clemmer. While there she designed and constructed home-built instruments, pushing the limits of the mobility resolution that can be obtained with a circular drift tube for the separation of biomolecules (peptides, proteins, carbohydrates, and metabolites). While there, she also studied hydrogen/deuterium exchange of proteins in the gas-phase as a function of time and pressure. Rebecca then went to Boston University as a Postdoctoral Associate in the lab of Professor Catherine Costello to develop a database containing collision cross section values for glycans, peptides, and glycopeptides utilizing Agilent Technologies 6560 IM-QTOF. This database can be used to determine how the collision cross section is altered with the addition of individual saccharide units. The trendlines obtained from this database will be used to predict collision cross sections for glycopeptides based on the conformation and structure of the specific glycoform.
</blockquote>
<blockquote>
Presenter: Jim Lau, PhD (HRAMS LC/MS Application Engineer, Agilent Technologies, Inc.)
</blockquote>
<blockquote>
Jim Lau received his Ph.D. From the University of Colorado. There he worked in the laboratories of Peter Albersheim and Robert Shapiro. This work involved the structure elucidation of plant natural products and, in particular, elucidating the structures of oligosaccharides derived from plant cell wall polysaccharides. This work was done in the early days of LCMS and made use of DLI-LCMS and (at the time) recently invented Thermospray-LCMS.
</blockquote>
<blockquote>
After the completion of his Ph.D., Jim joined Hewlett-Packard to work on LCMS ionization techniques with Paul Goodley during the early days of Electrospray-LCMS. He then moved to work on field applications and collaborations with Hewlett-Packard’s LCMS customers. More than 30 years later, Jim continues to work with Agilent’s customers in High Resolution Accurate Mass applications of LCMS. While involved in many areas of HRAMS LCMS, his recent work has focused on the area of Screening/Qual&amp;Quant of small molecules and on the high throughput confirmation of oligonucleotide synthesis.
</blockquote>

Agilent Technologies: How to set MS Scan Parameters for your LCMS Experiment

How to set MS Scan Parameters for your LCMS Experiment

An easy to follow guide detailing how to set MS scan parameters for an LCMS experiment will be presented.

The increasing complexity of the food supply chain, the exponential growth of chemical hazards and their regulations have brought several challenges to the field of food safety.
The need for productive gains and increased confidence in reporting non-compliant samples are particularly noteworthy challenges for laboratories that are routinely relied upon for maintaining a safe food supply chain. To meet these demands, mass spectrometric techniques such as tandem mass spectrometry and quadruple-time-of-flight mass spectrometry have emerged as the detectors of choice for the analysis of organic chemical hazards in foods and beverages.
One of the more recent significant developments is Shimadzu’s ultra fast family of mass spectrometric detectors that provide opportunities to increase both productivity and reporting confidence compared with more conventional mass spectrometric detectors. The importance of these state-of-the-art instruments to the analysis of chemical hazards in food will be discussed in the context of the regulatory requirements for the analysis of contaminants in foods and a general overview of chemical hazards in foods.
By viewing this webinar you will:
<ul>
<li>Understand the core challenges for food testing
</li>
<li>Recognize the key elements that can accelerate and streamline your workflow and increase your data confidence
</li>
<li>Learn and apply in various food safety analysis (e.g. multi-residual pesticides, veterinary drugs and mycotoxins).
</li>
</ul>
Who should view it?
<ul>
<li>Scientists and lab personnel conducting food analysis
</li>
<li>Lab managers in testing lab, regulatory agency and the food industry
</li>
<li>Everyone who is keen to increase their lab productivity and data confidence for food and beverage analysis.
</li>
</ul>
<blockquote>
Presdenter: Dr Peter Varelis (Applications Manager, Shimadzu Scientific Instruments (Oceania) )
</blockquote>
<blockquote>
Dr Peter Varelis has more than 20 years of research experience in both government and industry. He was also on an Elsevier editorial board (Food Chemistry and Analysis). His current research interest is the application of mass spectrometry to investigate organic compounds that have implications for human health and nutrition.
</blockquote>

Shimadzu: The Importance of Ultra Fast Mass Spectrometry for the Analysis of Chemical Hazards in Food & Beverages

The Importance of Ultra Fast Mass Spectrometry for the Analysis of Chemical Hazards in Food & Beverages

Understand the core challenges for food testing.

Ultra Fast Mass Spectrometry in Food & Beverages analysis

This exclusive Shimadzu Food Safety Webinar will provide an in-depth know-how about the various mass spectrometry (MS/MS) workflows that are needed to conduct high throughput pesticide analysis in challenging matrices.
You will learn about the latest state-of-the-art technologies that mass spec leaders are using globally to deal with pesticide analysis in difficult matrices such as spices and tobacco.
This webinar will be useful for anyone who is keen to learn about the latest advanced MS/MS technologies and will be particularly interesting for those who have faced difficulties while using challenging matrices.
By viewing this presentation you will learn...
<ul>
<li>about the practical aspects of MS/MS analysis using challenging matrices
</li>
<li>how these methods can be applied to such samples as spices and tobacco
</li>
</ul>
<blockquote>
Presenter: Dr Kaushik Banerjee
</blockquote>
<blockquote>
Dr Kaushik Banerjee is a National Fellow and Principal Scientist from the ICAR-National Research Centre for Grapes, Pune, India.
</blockquote>

Shimadzu: Spice Up Your Life with MS: Workflows for High Throughput Pesticide Analysis by MS/MS in Challenging Matrices such as Spices and Tobacco

Spice Up Your Life with MS: Workflows for High Throughput Pesticide Analysis by MS/MS in Challenging Matrices such as Spices and Tobacco

Know-how about the various mass spectrometry (MS/MS) workflows that are needed to conduct high throughput pesticide analysis in challenging matrices.

LCMS webinars focusing on LC/QQQ - page 23