<p><strong>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.</strong></p><h4><strong>In this episode, you'll learn:</strong></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><p>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.</p><h4><strong>Referenced Papers:</strong></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><p>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.</p><h3><strong>Video Transcription</strong></h3><h4><strong>From Structural Biology to Drug Discovery: Chromatography and Mass Spectrometry in Malaria Research</strong></h4><h5><strong>Introduction</strong></h5><p>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.</p><h5><strong>Research Focus: Malaria Drug Discovery and Kinase Targets</strong></h5><p>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.</p><p>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.</p><p>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.</p><h5><strong>Chromatography in Protein Expression and Purification Workflows</strong></h5><p>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.</p><p>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.</p><p>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.</p><h5><strong>Integrating Size Exclusion Chromatography into the Workflow</strong></h5><p>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.</p><p>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.</p><p>These iterative purification and troubleshooting steps are a routine part of protein biochemistry and reflect the importance of methodical optimization and careful validation.</p><h5><strong>The Role of Mass Spectrometry in Biomolecular Characterization</strong></h5><p>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.</p><p>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.</p><p>These approaches are essential for understanding how candidate drug targets function within complex biological systems.</p><h5><strong>Sample Preparation Challenges in Biological Research</strong></h5><p>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.</p><p>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.</p><h5><strong>Advances in Chromatography and MS for Malaria Research</strong></h5><p>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.</p><p>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.</p><p>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.</p><h5><strong>Malaria, Drug Resistance, and Global Impact</strong></h5><p>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.</p><p>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.</p><p>Understanding these molecular mechanisms is essential for developing robust, stage-specific antimalarial strategies.</p><h5><strong>Advice for Early-Career Researchers</strong></h5><p>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.</p><p>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.</p><p>Every successful experiment—no matter how small—represents meaningful progress and contributes to the broader goals of science and medicine.</p><h5><strong>Closing Remarks</strong></h5><p>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.</p><blockquote><p><strong>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.</strong></p></blockquote><blockquote><h4><strong>Concentrating on Chromatography Podcast</strong></h4><p>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!</p><p>You can find <strong>Concentrating on Chromatography Podcast </strong>in podcast apps:</p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL"><strong>Spotify</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185"><strong>Apple podcast</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography"><strong>podscan</strong></a></li></ul><p>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos"><strong>YouTube channel</strong></a></p></blockquote>

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

<p><strong>In the week of February 9, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.</strong></p><blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars"><strong>👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</strong></a></h4><p><strong>👉 Search and filter in the largest global database</strong> with over <strong>5 000 GC, LC, MS and spectroscopy webinars</strong>.</p></blockquote><h5><strong>1. SelectScience: High-Throughput Stability Screening Strategies for Antibody Formulation</strong></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><p>Learn how high-throughput DLS/SLS and rapid-screening DSC accelerate stability assessment of high-concentration antibody formulations, enabling faster, data-driven biologics development.</p><h5><strong>2. Phenomenex: Big Scale, Big Wins – Prep Chromatography Explained</strong></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><p>Learn how to scale analytical methods to preparative HPLC, optimize loading capacity, and understand the limits of preparative columns for pharmaceutical applications.</p><h5><strong>3. ALS Czech Republic: PFAS in Food &amp; Food Contact Material</strong></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><p>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.</p><h5><strong>4. New Food Magazine: The Science of Next-Gen Ingredients – Fermentation, Formulation and Function</strong></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><p>Explore how fermentation-driven innovation is transforming functional food ingredients and how advanced analytics optimize flavour, functionality, and stability.</p><h5><strong>5. SCIEX: Accurate Mass Fundamentals – Interpreting and Applying Your Data</strong></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><p>Session 3 focuses on interpreting and applying accurate mass data to confirm compound identity, move beyond basic quantitation, and troubleshoot results for confident reporting.</p><h5><strong>6. Agilent Technologies: Process Analytical Techniques – Online HPLC for Real-Time Monitoring and Control of Bioprocesses</strong></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><p>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.</p><h5><strong>7. Thermo Fisher Scientific: Introducing the Orbitrap Excedion Pro Hybrid MS</strong></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><p>Discover the new Orbitrap Exploris Pro with expanded ETD/EThcD capabilities for confident biopharmaceutical characterization, including intact proteins, PTMs, ADCs, and large biomolecules.</p><h5><strong>8. Waters Corporation: Planning Your NuGenesis Upgrade – Insights and Best Practices for a Smooth Transition</strong></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><p>Learn how to plan a successful NuGenesis upgrade, transition to Windows 11, and unlock new capabilities such as dashboards for real-time operational insights.</p><h5><strong>9. Thermo Fisher Scientific: Comprehensive Analytical Strategies for Peptide Therapeutics and GLP-1 Agonists with Agilent</strong></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><p>Explore analytical workflows for peptide therapeutics, including method development, peptide mapping, GLP-1 QC, and LC-MS strategies across Agilent platforms.</p><h5><strong>10. Agilent Technologies: Moving from R&amp;D and Limited QC on a UV-Vis-NIR Instrument to Large-Scale QC Using an Autosampler</strong></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><p>This webinar covers practical aspects of adding and using an autosampler to maximize UV-Vis-NIR QC workflows at scale.</p><h5><strong>11. Agilent Technologies: LC Method Transfer – Hidden Challenges &amp; Absolute Solution</strong></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><p>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.</p>

Webinars LabRulezLCMS Week 07/2026

<p><strong>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.</strong></p><p>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.</p><blockquote><h4><strong>The original article</strong></h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771"><strong>Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology</strong></a></h4><p>Robert L. Rider, Jared Hampton, Zhenyu Xi, Carter Lantz, Sangho D. Yun, Weijing Liu, Rosa Viner, Arthur Laganowsky, and David H. Russell*</p><p>Anal. Chem. 2025, 97, 49, 27057–27063</p><p><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.analchem.5c05771">https://doi.org/10.1021/acs.analchem.5c05771</a></p><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/"><strong>CC-BY 4.0</strong></a></h6></blockquote><p><strong>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.</strong></p><p>Transthyretin (TTR) is a homotetrameric transport protein that circulates in plasma and cerebrospinal fluid, delivering thyroxine (T<sub>4</sub>) 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.</p><p>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></p><p>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 <i>m</i>/<i>z</i> 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 <i>m</i>/<i>z</i> 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></p><p>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 (<i>m</i>/<i>z</i> × 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.</p><h4><strong>Experimental Section</strong></h4><h5><strong>Data Collection</strong></h5><p>All experiments were conducted on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/560"><strong>Thermo Scientific Q-Exactive UHMR</strong></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.</p><h4><strong>Results and Discussion</strong></h4><p>CDMS has emerged as a powerful tool for analyzing heterogeneous biomolecular samples, enabling accurate, direct mass determination by simultaneously measuring the charge and <i>m</i>/<i>z</i> 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 <i>m</i>/<i>z</i>). <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 T<sub>4</sub> bound states of both WT- and CT-TTR tetramers, where &lt;3900 <i>m</i>/<i>z</i> has observable separation between all proteoforms. However, for the 14+ and 15+ charge states of WT- and CT-TTR, respectively, the 0 T<sub>4</sub>- and 1 T<sub>4</sub>-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<sup>+</sup>, K<sup>+</sup>, and Zn<sup>2+</sup>) 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 <i>m</i>/<i>z</i> overlap to resolve and quantify hybrid tetramer formation and T<sub>4</sub> binding.</p><p><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"></p><h5><strong>Thyroxine Binding to TTR Homotetramers</strong></h5><p>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 T<sub>4</sub> into T<sub>3</sub> (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 T<sub>4</sub> 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 T<sub>4</sub>) 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 T<sub>4</sub>.</p><p>DMT was further applied to quantify T<sub>4</sub> 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 T<sub>4</sub>. While ligand-bound species can be observed, homotetramers cannot be confidently resolved across the entire 3000–5000 <i>m</i>/<i>z</i> 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 <i>m</i>/<i>z</i> by separating the 14+ and 15+ charge states for WT and CT, respectively, in the range 3900–4200 <i>m</i>/<i>z</i>. 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 <i>m</i>/<i>z</i> yet differ in mobility, CDMS could be an alternative or used complementarily since the species likely also differ in charge.</p><p><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"></p><h4><strong>Conclusion</strong></h4><p>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 T<sub>4</sub> 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.</p><p>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 <i>m</i>/<i>z</i> 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 <i>m</i>/<i>z</i> 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></p>

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

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Waters SELECT SERIES Cyclic IMS

The SELECT SERIES Cyclic IMS combines novel cyclic ion mobility separation with state-of-the-art, high performance, time-of-flight mass spectrometry.

<div><div id="title-c6692d35e8" data-locator="title-with-text"><h3><strong>Endless possibilities. Limitless research.</strong></h3></div></div><div><div id="text-ba9d3d94da" data-locator="text"><p><strong>Developed through focused collaboration, the SELECT SERIES Cyclic IMS combines novel cyclic ion mobility separation with state-of-the-art, high performance, time-of-flight mass spectrometry, enabling leading researchers to unlock the potential in scientific discovery.</strong></p><p>The SELECT SERIES Cyclic IMS enables selection of ions by both mass and mobility, a unique functionality of <strong>Cyclic Ion Mobility (cIM)</strong> that provides unparalleled flexibility and capabilities for research studies in both academia and industry. With ion mobility and mass spectrometry, you can separate by shape as well as&nbsp;<i>m/z</i>&nbsp;for separation of isomers, measure the <strong>Collisional Cross Section (CCS)</strong> of an ion, and achieve significantly cleaner mass spectral data.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_SELECT_SERIES_Cyclic_IMS_Novel_Cyclic_Ion_Mobility_c_IM_Technology_13abf6dd9b.jpg" alt="Waters SELECT SERIES Cyclic IMS: Novel Cyclic Ion Mobility (cIM) Technology." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_SELECT_SERIES_Cyclic_IMS_Novel_Cyclic_Ion_Mobility_c_IM_Technology_13abf6dd9b.jpg 234w," sizes="100vw" width="1024" height="682"></p><h3><strong>Overview</strong></h3><div data-locator="section-container-body"><div><div><div data-locator="layoutcontainer-"><div><div id="text-26eab4b89b" data-locator="text"><ul><li>Combine <strong>cyclic ion mobility (cIM) separation</strong> with <strong>ToF mass spectrometry</strong></li><li>Separate more than ever before with ultimate ion mobility resolution for complete confidence</li><li>Perform <strong>unique IMS<sup>n</sup> experiments</strong> for increased selectivity and advanced characterization</li><li>Enable <strong>pre-mobility mass selection</strong> and <strong>mobility selection of precursor and product ions</strong></li><li>Achieve increased experimental flexibility for solving complex problems with three distinct fragmentation regions</li></ul></div></div><div><div id="text-36ff553b5f" data-locator="text"><h3><strong>Recommended Use</strong></h3><p>For identifying and rapidly monitoring co-eluting, isomeric metabolites in chemical reactions</p><blockquote><p class="cke-user_style-important"><strong>Video: </strong><a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/watch?v=nauwVH0L91o"><strong>Waters SELECT SERIES Cyclic IMS</strong></a></p></blockquote><div><div id="text-8469d7776e" data-locator="text"><h3 data-locator="modal-title"><strong>Discover more with ultimate ion mobility resolution</strong></h3><p>The instrument design and control software enable a range of experiments, including acquisition of Tof data, Single pass ion mobility, and the ability to scale mobility resolution to match the complexity of a sample. Ion mobility resolution increases with the length of the mobility device and therefore with the number of passes.</p><figure class="image"><img style="aspect-ratio:1024/682;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_SELECT_SERIES_Cyclic_IMS_IMS_resolution_increases_with_the_number_of_passes_around_the_c_IM_device_121719dbe0.jpg" alt="Waters SELECT SERIES Cyclic IMS: IMS resolution increases with the number of passes around the cIM device. Demonstrated here by the separation of reverse sequence peptides SDGRG and GRGDS. The Arrival Time Distributions (ATDs) obtained after 100 passes around the device are inset." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_SELECT_SERIES_Cyclic_IMS_IMS_resolution_increases_with_the_number_of_passes_around_the_c_IM_device_121719dbe0.jpg 234w," sizes="100vw" width="1024" height="682"></figure><div><div id="text-bb2fb9f91c" data-locator="text"><h3 data-locator="modal-title"><strong>Unlock the potential in scientific discovery</strong></h3><p>The unique instrument design of the SELECT SERIES Cyclic IMS&nbsp;facilitates advanced ion mobility experiments like IMS<sup>n</sup>&nbsp;isolation. IMS<sup>n</sup>&nbsp;isolation&nbsp;extends the resolution of a specific mobility range,&nbsp;<i>e.g.,</i>&nbsp;ions of a specific species. Eject ions (without acquisition) outside of the desired mobility range, leaving the remaining species in the cIM to continue the separation process. This “trimming” approach can be undertaken numerous times and can be used, for example, to increase specificity of the selected ions or to prevent “wrap-around” in the cIM where high mobility ions catch up with low mobility ions in multi-pass experiments. Multiple cyclic sequences of different numbers of passes can be defined in one, multi-pass LC-MS method, increasing productivity by reducing the need for multiple injections of the same sample.</p></div></div><figure class="image"><img style="aspect-ratio:1024/578;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_SELECT_SERIES_Cyclic_IMS_Investigation_into_acyl_glucuronides_via_infusion_f3bf2c67e2.jpg" alt="Waters SELECT SERIES Cyclic IMS: Investigation into acyl glucuronides via infusion. Slicing enables further IMS separation of target metabolite (blue region) of interest and other ions can be ejected. Increasing the IMS resolution reveals an additional 4-O acyl. In collaboration with Imperial College London – Ian D. Wilson." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_SELECT_SERIES_Cyclic_IMS_Investigation_into_acyl_glucuronides_via_infusion_f3bf2c67e2.jpg 245w," sizes="100vw" width="1024" height="578"></figure><div><div id="text-78a4dc4d5e" data-locator="text"><h3 data-locator="modal-title"><strong>Undertake advanced structural characterization</strong></h3><p><strong>IMS<sup>n</sup>&nbsp;activation</strong>&nbsp;is ideal for <strong>advanced structural characterization</strong>. During mobility separation, excise a segment of the mobility separated species and send the ions to the pre array storage device. Unwanted ions are ejected, and the stored ions are then re-injected into the array under collision induced activation/dis-sociation conditions, as required, and subsequent mobility separation performed. The product ions can then be sent to the&nbsp;Tof<i>&nbsp;</i>for detection or can undergo further rounds of mobility selection providing the unique IMS<sup>n</sup>&nbsp;capability.</p></div></div><div><div id="text-079d02ceb8" data-locator="text"><h3 data-locator="modal-title"><strong>Imaging mass spectrometry with DESI XS and Cyclic IMS</strong></h3><p>The unique combination of&nbsp;<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?instrumentationItems=26&amp;mainauthorItems=5&amp;search=DESI+XS"><strong>DESI XS</strong></a><strong>&nbsp;</strong>with SELECT SERIES Cyclic IMS provides ultimate levels of specificity for <strong>MS imaging</strong> approaches. DESI XS produces a visual map of the spatial distribution of a wide range of analytes, for example small molecule drugs, metabolites, and lipids across the surface of a tissue sample, and the unique capabilities and modes of acquisition of Cyclic IMS enable comprehensive in-depth experiments to be performed.</p></div></div><div><div id="text-673d117887" data-locator="text"><h3 data-locator="modal-title"><strong>Increased sensitivity provides confidence in what you find</strong></h3><p>To complement the novel <strong>Cyclic Ion Mobility</strong> capability and for complete confidence in your data, the&nbsp;SELECT SERIES&nbsp;Cyclic IMS is equipped with the latest <strong>ToF technology</strong>. The XS transfer device maintains the fidelity of the ion mobility separation while simultaneously conditioning the ion beam for the absolute best time-of-flight performance. The new offset oa-Tof with dual gain detection system <strong>provides improved sensitivity, resolution &gt;100,000 (FWHM), reliable accurate exact mass measurements</strong> (low ppm), and <strong>improved dynamic range</strong>.</p><figure class="image"><img style="aspect-ratio:1024/682;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Mass_spectrum_highlighting_resolution_of_100_000_FWHM_on_the_7_charge_state_of_monomeric_9ff8f53204.jpg" alt="Waters SELECT SERIES Cyclic IMS: Mass spectrum highlighting resolution of >100,000 (FWHM) on the 7+ charge state of monomeric." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Mass_spectrum_highlighting_resolution_of_100_000_FWHM_on_the_7_charge_state_of_monomeric_9ff8f53204.jpg 234w," sizes="100vw" width="1024" height="682"></figure></div></div></div></div></div></div></div></div></div></div></div></div>

Waters SYNAPT XS High Resolution Mass Spectrometer

The SYNAPT XS Ion Mobility Time-of-Flight Mass Spectrometer provides ultimate flexibility, offering greater freedom of analytical choice to support scientific creativity and technical success for any application.

<div><div><h4><strong>Ultimate flexibility for deeper discovery</strong></h4></div></div><div><div><p><strong>In the arena of scientific discovery, the slow pace of advancement and escalating costs of research can prove to be a challenge. Unlike competitor systems with restricted inlet options, scan function limitations, or requiring multiple platforms, only Waters offers an all-encompassing high-performing LC-MS solution, the SYNAPT XS mass spectrometer, for ultimate flexibility and greater freedom of analytical choice – supporting scientific creativity and technical success for any application.</strong></p><ul><li><strong>Novel technology building blocks deliver cutting-edge analytical performance</strong></li><li><strong>SONAR</strong> and <strong>HDMSE</strong> provide a unique toolkit for interrogating complex mixtures</li><li><strong>Ion mobility</strong> multiplies peak capacity and selectivity of analysis</li><li><strong>CCS measurements</strong> increase security of compound identification</li><li><strong>Deeper discovery in Mass Spectrometry Imaging</strong> with<strong> </strong><a target="_blank" rel="noopener noreferrer" href="https://www.waters.com/waters/Full-Spectrum-Molecular-Imaging-/nav.htm?cid=135070661"><strong>Full Spectrum Molecular Imaging</strong></a> enabled by <a target="_blank" rel="noopener noreferrer" href="https://www.waters.com/waters/DESI-XS---Desorption-Electrospray-Ionization-/nav.htm?cid=135047466"><strong>DESI XS</strong></a> and MALDI</li></ul><h4><strong>Overview</strong></h4><div><div><div><div><ul><li><strong>Serve the broadest range of applications </strong>with the most extensive range of chromatograph inlets for ultimate flexibility</li><li><strong>Attain fragment ion information for every detectable component</strong> for unambiguous confirmation of compound identity with DIA modes <strong>SONAR</strong>, MSE, and <strong>HDMSE</strong></li><li><strong>Generate rich fragmentation data</strong> from highly complex samples in all acquisition modes including DDA</li><li>Simplify and streamline the mass spectral imaging workflow and deliver multi-layered, information-rich data with multiple imaging techniques and accompanying High Definition Imaging (HDI) Software</li><li><strong>Achieve automated higher order structure determination </strong>thorough confident identification, intact mass analysis, and best-in-class reproducibility</li><li><strong>Enhance MS/MS possibilities</strong> using complementary fragmentation techniques with high resolution and accurate mass measurements</li></ul></div></div><div><div><h5><strong>Recommended Use</strong></h5><p>For deeper discovery by aligning complimentary workflows on a single <strong>Ion mobility</strong> enabled time-of-flight mass spectrometer with the flexibility of multiple ion sources and acquisition modes.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_SYNAPT_XS_High_Resolution_Mass_Spectrometer_4_696d77ce2b.jpg" alt="Waters SYNAPT XS High Resolution Mass Spectrometer: The Waters SYNAPT XS offers flexibility and freedom of analytical choice with an extensive range of chromatographic inlets." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_SYNAPT_XS_High_Resolution_Mass_Spectrometer_4_696d77ce2b.jpg 234w," sizes="100vw" width="1024" height="682"></p><div><div><h3><strong>Cutting edge performance with novel technology</strong></h3><p>With technology building blocks inherited from the <strong>Waters Advanced Mass Spectrometry</strong> <strong>SELECT SERIES</strong>, advanced innovation is built-in, ensuring scientists using this platform are at the cutting edge of mass spectrometry while retaining the ease of use and established end-to-end workflows for which the <strong>SYNAPT </strong>is well known.</p><ul><li><strong>StepWave&nbsp;XS -&nbsp;</strong>Redesigned segmented quadrupole transfer optics provide enhanced sensitivity for challenging compounds while further improving levels of analytical robustness.</li><li><strong>Extended ToF -&nbsp;</strong>Delivers UPLC-compatible mass resolution, matrix-tolerant dynamic range, and quantitative results for the most complex samples, while offering superior specifications to previous SYNAPT models.</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_SYNAPT_XS_High_Resolution_Mass_Spectrometer_9f19abb382.jpg" alt="Waters SYNAPT XS High Resolution Mass Spectrometer: SYNAPT XS schematic." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_SYNAPT_XS_High_Resolution_Mass_Spectrometer_9f19abb382.jpg 245w," sizes="100vw" width="1024" height="546"></p></div></div><div><div><h3><strong>Interrogate complex mixtures with a unique toolkit</strong></h3><p>A complete analytical strategy requires the combination of appropriate complementary techniques to see the bigger picture. With both <strong>SONAR</strong> and IMS-based <strong>data independent acquisition</strong> (DIA) modes of operation on the SYNAPT XS, the discovery analyst is in a unique position to interrogate complex mixtures by complementary mechanisms. Both types of acquisition increase analytical <strong>peak capacity</strong>, providing ‘clean and clear’ fragmentation data, but based on different molecular properties. This provides a truly unique investigative toolbox for the in-depth interrogation of complex mixtures.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_SYNAPT_XS_High_Resolution_Mass_Spectrometer_2_9179e575a4.jpg" alt="Waters SYNAPT XS High Resolution Mass Spectrometer: During each scan the quadrupole separates co-eluting precursor masses by scanning the mass range, and transiting them in sequence. Fragment ions from different precursors can then be recorded separately and assigned with confidence." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_SYNAPT_XS_High_Resolution_Mass_Spectrometer_2_9179e575a4.jpg 245w," sizes="100vw" width="1024" height="593"></p></div></div><div><div><h3><strong>Discover more with ion mobility and CSS measurement</strong></h3><p>Conventional mass spectrometers separate components based on m/z. The SYNAPT XS also allows separation of molecules according to<strong> their size, shape, and charge during ion mobility experiments as a function of their collisional cross section</strong> (CCS). As well as ion mobility offering an additional dimension of resolution, multiplying <strong>peak capacity</strong>, and <strong>selectivity of analysis</strong> the measurement of CCS offers additional molecular identifiers. The measured CCS of an ion can be used to help confirm an ion’s identity or investigate its structure. The inclusion of ion mobility significantly increases the extent and confidence with which a scientist can profile complex mixtures and complex molecules – dramatically enhancing sample definition.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_SYNAPT_XS_High_Resolution_Mass_Spectrometer_3_2240bff527.jpg" alt="Waters SYNAPT XS High Resolution Mass Spectrometer: Retention and drift time principle ion mobility enabled data-independent LC-HDMSE analysis (LC-DIA-IM-MS)." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_SYNAPT_XS_High_Resolution_Mass_Spectrometer_3_2240bff527.jpg 204w," sizes="100vw" width="1024" height="784"></p></div></div><div><div><h3><strong>Achieve ultra-confident structural characterization of components</strong></h3><p>Time aligned parallel (TAP) fragmentation is an acquisition mode unique to the T-Wave IMS design. It permits users to take the advantage of the <strong>TriWave configuration</strong>, which allows the pre-IMS T-Wave and post-IMS T-Wave to operate as two separate collision cells. The resultant CID-IMS-CID instrumental operation helps to provide ultra-confident structural characterization of components. <strong>TAP fragmentation</strong> provides a distinct advantage for building a complete structure, through superior fragment ion coverage, sensitivity, and accuracy compared to traditional MSⁿ or MS/MS techniques.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_SYNAPT_XS_High_Resolution_Mass_Spectrometer_5_4dd33f1ab5.jpg" alt="Waters SYNAPT XS High Resolution Mass Spectrometer: Schematic showing Time Aligned Parallel Fragmentation. " srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_SYNAPT_XS_High_Resolution_Mass_Spectrometer_5_4dd33f1ab5.jpg 234w," sizes="100vw" width="1024" height="682"></p></div></div></div></div></div></div></div></div>

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