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X-WR-CALDESC:Events for Department of Chemical Engineering
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DTSTART;TZID=America/New_York:20260508T130000
DTEND;TZID=America/New_York:20260508T140000
DTSTAMP:20260608T213850
CREATED:20260504T135009Z
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SUMMARY:ChE PhD Dissertation Defense: Kevin Yang
DESCRIPTION:Name:\nKevin Yang \nTitle:\nStructural Investigation of Single-Atom Catalysts in HCl Electrolysis\, CO₂ Reduction\, and Li-S Batteries \nDate:\n05/08/2026 \nTime:\n01:00:00 PM \nCommittee Members:\nProf. Sanjeev Mukerjee (Advisor)\nProf. Joshua Gallaway\nProf. Hannah Sayre\nProf. Magda Barecka \nLocation:\nEXP 202 \nAbstract:\nTransition metal single-atom catalysts have emerged as a promising class of materials for electrochemical energy conversion and storage due to their high atomic utilization\, tunable electronic structure\, well-defined active sites\, and use to high earth abundant metals. Metal nitrogen carbon (M-N-C) catalysts are practical in a wide range of electrochemical systems. However\, the development of M-N-C catalysts into industrial systems still requires much effort\, in part\, due to the lack of durability and stability studies. M-N-C catalysts can be used in oxygen depolarized cathode (ODC) HCl electrolysis\, CO2 reduction\, and lithium sulfur (Li-S) batteries. Understanding the mechanisms of M-N-C degradation\, durability\, and effects of modifications to such catalysts would ultimately benefit their implementation in each electrochemical system.   Chapter 1 introduces M-N-C catalysts and the various electrochemical systems they will be used in (ODC HCl electrolysis\, CO2 reduction\, and Li-S batteries). \nIn chapter two\, we investigate the durability of the Fe-N-C catalyst in ODC HCl electrolysis. Fe-N-C exhibits high oxygen reduction activity and strong resistance to chloride poisoning relative to most noble metal catalysts. However\, its durability and degradation mechanisms in HCl electrolysis are not well studied. Through a combination of durability studies\, accelerated stress tests\, and multimodal spectroscopic techniques\, we identified two main degradation pathways: an operational demetallation of Fe-N4 active sites under sustained polarization and a carbon-corrosion-induced demetallation that occurs during the transient conditions of uncontrolled shutdown. Spectroscopic analysis reveals one unstable FeN4 moiety and two stable Fe-N-C moieties that can withstand the HCl electrolysis operating conditions. These findings establish a mechanism for Fe-N-C degradation to drive future catalyst design. \nIn chapter three\, we modify Fe-N-C catalyst and Ni-N-C catalyst with heteroatom dopants to observe their effects on CO2 reduction activity\, product selectivity\, and the correlation with the changes in electronic and coordination structure. Using a post-pyrolysis treatment process\, we dope the environment around the metal active center either by introducing an axial ligand or binding to the carbon structure. Utilizing in situ/operando XAS\, we found that the dopants are generally not stable and can introduce a site-blocking effect at low overpotentials. Through these findings\, we find that the axial ligand dopants are not durable during CO2 reduction and do not make large contributions to the activity or product distribution of Ni-N-C and Fe-N-C in CO2 reduction. \nIn chapter four\, we investigate the effects of metal centers for M-N-C in polysulfide conversion and the changes in the active site structure after operation. The catalytic activity of M-N-C catalysts varies largely with different metal centers and coordinating environments.  We find that Co-N-C and Fe-N-C favor the oxidation of short-chain polysulfides to elemental sulfur\, while Sn-N-C and Ni-N-C make a larger contribution to the reduction of elemental sulfur to short-chain polysulfides. Mo-N-C\, which had the presence of Mo nanoparticles\, exhibited the lowest increase in performance compared to the others. This finding emphasizes the catalytic capability and importance of synthesizing purer M-N-C catalysts. All M-N-C catalysts were able to impact the conversion of lithium polysulfides to gain performance greater than baseline carbon. X-ray spectroscopic methods were used to analyze the structure of the M-N-C catalyst at various cycles to find that the active site structure of Fe-N-C undergoes a partial change to form Fe2O3\, while Co-N-C and Ni-N-C remain relatively stable. This change in the active site could be a cause of capacity decay in Li-S batteries. \nChapter 5 summarizes the findings and offers suggestions for future work. \n\nKevin Yang is a Ph.D. candidate in Chemical Engineering at Northeastern University\, where his research focuses on understanding structure–property relationships in single-atom catalysts for electrochemical energy conversion and storage. His work spans multiple electrochemical systems\, including oxygen depolarized cathodes for hydrochloric acid electrolysis\, CO₂ electroreduction\, and lithium–sulfur batteries\, with an overarching emphasis on how catalyst active sites evolve under operating conditions and how those structural changes govern activity\, selectivity\, and durability. Kevin’s research combines electrochemical engineering with advanced multimodal characterization\, including in situ and ex situ X-ray absorption spectroscopy (XANES/EXAFS)\, X-ray photoelectron spectroscopy\, Raman spectroscopy\, electron microscopy\, and electrochemical diagnostics. Through this work\, he has developed mechanistic insights into active site degradation pathways in Fe–N–C and other transition metal–nitrogen–carbon single-atom catalysts\, helping bridge fundamental catalyst chemistry with practical reactor operation.
URL:https://che.northeastern.edu/event/che-phd-dissertation-defense-kevin-yang/
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DTSTART;TZID=America/New_York:20260603T140000
DTEND;TZID=America/New_York:20260603T160000
DTSTAMP:20260608T213850
CREATED:20260527T193616Z
LAST-MODIFIED:20260527T193616Z
UID:6092-1780495200-1780502400@che.northeastern.edu
SUMMARY:Chemical Engineering GSC CV/Resume Workshop
DESCRIPTION:The Chemical Engineering Graduate Student Council is inviting fellow students to attend an upcoming CV/Resume Workshop designed to help you strengthen your academic and professional applications. \nPlease RSVP \nThis workshop will cover: \n\nResume and CV formatting\nTailoring applications for internships\, fellowships\, and jobs\nCommon mistakes to avoid in CV/Resume\n\nWe encourage all graduate students to attend and take advantage of this opportunity to improve their professional documents.
URL:https://che.northeastern.edu/event/chemical-engineering-gsc-cv-resume-workshop/
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DTSTART;TZID=America/New_York:20260624T123000
DTEND;TZID=America/New_York:20260624T133000
DTSTAMP:20260608T213850
CREATED:20260608T185600Z
LAST-MODIFIED:20260608T185600Z
UID:6108-1782304200-1782307800@che.northeastern.edu
SUMMARY:ChE PhD Dissertation Defense: Natesan Mani
DESCRIPTION:Name:\nNatesan Mani \nTitle:\nA Tale of Two Fcs: Investigating Furin cleavage in the SARS-CoV-2 Spike Protein and Glycan Effects in IgG Fcs \nDate:\n06/24/2026 \nTime:\n12:30:00 PM \nCommittee Members:\nProf. Srirupa Chakraborty (Advisor)\nProf. Francisco Hung\nProf. Sunny Zhou\nDr. Alla Polozova \nLocation:\n409 Robinson Hall \nAbstract:\nThis dissertation examines critical structural dynamics in viral infection and antibody-mediated immune response using Molecular Dynamics (MD) simulations. We investigated two distinct but fundamentally related systems: the SARS-CoV-2 Spike protein with emphasis on Furin cleavage (the antigen Fc)\, and the IgG1 Fc-CD16a receptor interaction with varying glycosylation profiles (the antibody Fc). \nAntigen Study: The SARS-CoV-2 Spike protein’s furin cleavage site (FCS) is a defining feature that distinguishes it from its predecessor SARS-CoV and is critical to viral infectivity. While extensive vaccine research has utilized stabilized Spike constructs with mutated or deleted FCS\, physiologically\, the cleavage occurs during viral particle formation. Using large-scale atomistic MD simulations of both Furin Cleaved and Uncleaved Spike proteins in the receptor-binding domain (RBD) Open and Closed conformations\, we demonstrate that furin cleavage fundamentally alters the Spike protein’s conformational dynamics. We observe increased correlated motions between the RBD and N-terminal domain (NTD) in the Furin Cleaved systems\, enhanced RBD sampling of exposed conformations favorable for ACE2 binding and altered glycan clustering patterns on key N-linked glycans. These observations provide quantitative evidence that cleavage primes the Spike protein for membrane fusion and enhances receptor accessibility. These findings provide a mechanistic foundation for designing immunogens and therapeutics targeting not only SARS-CoV-2 but also emerging Sarbecoviruses and related viral families. \nAntibody Study: IgG1 is the predominant antibody subclass used in therapeutic applications\, with its Fc region mediating critical effector functions including antibody-dependent cellular cytotoxicity (ADCC) through CD16a receptor engagement on natural killer cells. The glycosylation profiles of both the IgG1 Fc and CD16a receptor play essential roles in determining binding affinity and immune response magnitude. Using MD simulations of 22 distinct glycoform combinations\, we systematically examine how variations in core fucosylation and terminal galactosylation affect Fc-CD16a complex formation and stability. We evaluate the structural impact of asymmetric binding between the two Fc arms and the receptor\, calculate binding affinities and correlate structural observations with binding energetics. Our results validate known trends (afucosylation enhancement) while revealing nuanced effects of galactosylation and chain-specific glycan positioning. Together\, these findings and the accompanying mechanistic framework provide a foundation for the glycan-informed rational design of next-generation antibody therapeutics with enhanced immune potency \nTogether\, these studies demonstrate how atomistic molecular dynamics can bridge gaps between structural biology and functional outcomes\, providing quantitative frameworks for designing improved viral vaccines and enhanced therapeutic antibodies. The methodologies and insights presented here have broad applicability to understanding glycoprotein-receptor interactions across biological systems. \n\nNatesan Mani is a PhD candidate in Chemical Engineering at Northeastern University\, where he expects to defend in June 2026. He completed his M.S. in Chemical Engineering at the University of Houston in 2020 and earned his B.S. in Chemical Engineering from Osmania University in India in 2019. His doctoral research in the SimBioSys Lab at Northeastern University focuses on developing physics-informed computational tools that combine molecular dynamics (MD) simulations and machine learning to predict molecular properties and guide the design of high-affinity antibodies\, work conducted in direct collaboration with Amgen’s Pivotal Attribute Sciences team. Natesan has gained significant industry experience through internships at Amgen\, where he modeled antibody-receptor interfaces and developed GPU-accelerated simulation pipelines\, and at Prescient Design (Genentech)\, where he built multi-modal biological data frameworks to inform therapeutic design decisions. He has authored one first-author manuscript in Protein Science\, has two manuscripts under review\, and has presented his research at over five national conferences\, including BPS\, AIChE\, and ACS. He is also the creator of F.A.D.E (Fully Agentic Drug Engine)\, a prize-winning integrated modelling framework recognized at the Broad Institute ML Symposium and selected for presentation at ACS SciMix and ACS COMP. Beyond his research\, Natesan is an active leader in his academic community. He founded the Northeastern Biophysical Society student chapter and served as its President in 2025. He also served as a Treasurer of the ChemE Graduate Student Council. He has been recognized with numerous honours\, including the LEADERs Fellowship\, NSF ACCESS Award\, multiple travel grants and recognition from both the Department of Chemical Engineering and the University.
URL:https://che.northeastern.edu/event/che-phd-dissertation-defense-natesan-mani/
LOCATION:409 Robinson Hall\, 360 Huntington Ave\, 409 RB\, Boston\, MA\, 02115\, United States
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