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X-WR-CALDESC:Events for Department of Chemistry
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DTSTART;TZID=America/New_York:20260203T110000
DTEND;TZID=America/New_York:20260203T115000
DTSTAMP:20261001T181125
CREATED:20250812T203701Z
LAST-MODIFIED:20260122T220656Z
UID:2251-1770116400-1770119400@inside.wooster.edu
SUMMARY:Chemistry and BCMB Seminar
DESCRIPTION:Sara E. S. Martin\, PhD\, Associate Professor\, Chemistry; Biochemistry & Molecular Biology\, The College of Wooster\n\n\n\n“Molecular Makeovers: From Simple Precursors to Bio‑Relevant Heterocycles”\n\n\n\n\n\n\n\nQuinolinones and coumarins are related nitrogen- and oxygen-containing heterocycles that appear in a variety of bioactive molecules\, including pH probes\, natural products\, and pharmaceuticals. Despite their importance\, certain isomers of these molecules are hard to make. Most current synthetic routes to access 7-substituted quinolinones and coumarins either work for only a narrow set of starting materials or require multiple steps that change oxidation states after the molecule’s carbon framework is already built. These approaches limit how easily chemists can explore new structures. \n\n\n\nResearch in the Martin lab has taken a different strategy to build quinolinones\, forming the carbon skeleton from simpler building blocks using a two-step reaction sequence that converts meta‑substituted anilines and methyl 3\,3‑dimethoxypropionate to mainly 7‑substituted quinolinones. This seminar will discuss recently published studies aimed at understanding what controls the ratio of the two isomeric products and more recent work aimed at 1) developing milder reaction conditions for this transformation  2) synthesizing interesting biologically relevant quinonliones\, and 3) optimizing reaction conditions for coumarin synthesis. \n\n\n\n\n\nLocation: Ruth W. Williams Hall of Life Sciences\, Room 060
URL:https://inside.wooster.edu/chemistry/event/chemistry-and-bcmb-seminar/
CATEGORIES:BCMB,Chemistry,Seminars,Seniors,STEM Success Initiative
ATTACH;FMTTYPE=image/jpeg:https://inside.wooster.edu/chemistry/wp-content/uploads/sites/59/2025/08/Group-photo-scaled.jpg
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BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260210T110000
DTEND;TZID=America/New_York:20260210T115000
DTSTAMP:20261001T181125
CREATED:20250812T145609Z
LAST-MODIFIED:20250812T150032Z
UID:2229-1770721200-1770724200@inside.wooster.edu
SUMMARY:Chemistry Seminar
DESCRIPTION:Casey Wade\, Associate Professor\, The Ohio State University\n\n\n\nLocation: Ruth W. Williams Hall of Life Sciences\, Room 045
URL:https://inside.wooster.edu/chemistry/event/chemistry-seminar-4/
CATEGORIES:Chemistry,Seminars,Seniors,STEM Success Initiative
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260224T110000
DTEND;TZID=America/New_York:20260224T115000
DTSTAMP:20261001T181125
CREATED:20250812T203951Z
LAST-MODIFIED:20260217T133023Z
UID:2253-1771930800-1771933800@inside.wooster.edu
SUMMARY:Chemistry New Major Gathering
DESCRIPTION:Welcome Class of 2028\n\n\n\n\n\nLocation: Severance Hall\, Room 105 (STEM Zone)
URL:https://inside.wooster.edu/chemistry/event/chemistry-seminar-5/
CATEGORIES:Chemistry
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260303T110000
DTEND;TZID=America/New_York:20260303T115000
DTSTAMP:20261001T181125
CREATED:20250812T150004Z
LAST-MODIFIED:20260226T203118Z
UID:2231-1772535600-1772538600@inside.wooster.edu
SUMMARY:Chemistry & BCMB Seminar
DESCRIPTION:Xiohong Tan\, Assistant Professor\, Bowling Green State University\n\n\n\n\n\nEfficient Blockade of the PD-1/PD-L1(2) Axis via Novel Chemical Inhibitors\n\n\n\n\n\n\n\nLocation: Ruth W. Williams Hall of Life Sciences\, Room 060 \n\n\n\nLunch RSVP: Sign up \n\n\n\nAbstract:\n\n\n\nUnderstanding protein–protein interactions (PPIs) is central to deciphering cellular processes\, as proteins are the primary functional molecules within cells. Peptides and aptamers\, which occupy a strategic niche between antibodies and small molecules\, have emerged as powerful tools for probing and modulating PPIs. \n\n\n\nPeptides serve as highly versatile ligands\, recognizing proteins through hydrogen bonding\, van der Waals forces\, and ionic interactions. They can be chemically synthesized at low cost\, possess low molecular weight\, and exhibit enhanced tissue and cellular penetration\, making them highly attractive for both research and therapeutic applications. Aptamers\, short single-stranded RNA or DNA molecules\, fold into unique three-dimensional structures that enable tight\, highly specific binding to diverse molecular targets. As compelling alternatives to antibodies\, aptamers—especially DNA-based ones—offer long shelf life\, low toxicity\, minimal immunogenicity\, cost-effective chemical synthesis\, and broad tolerance for chemical modifications\, positioning them as versatile candidates for diagnostics\, targeted therapy\, and drug development. \n\n\n\nIn this talk\, I will present our recently developed aptamers and peptides targeting the PD-1/PD-L1(2) axis. These novel ligands provide a next-generation strategy for modulating PPIs\, opening new avenues for therapeutic intervention and translational applications in immuno-oncology. \n\n\n\nBio:\n\n\n\nDr. Xiaohong Tan earned his Ph.D. from Nanyang Technological University\, Singapore. After completing postdoctoral training at the Center for Nucleic Acids Science and Technology at Carnegie Mellon University\, USA\, he began his independent research career in the Department of Chemistry at Bowling Green State University\, USA\, where he was promoted to Associate Professor with tenure in 2025. His research expertise encompasses nucleic acid chemistry\, peptide chemistry\, and protein biochemistry\, with a particular focus on developing aptamer- and peptide-based probes for precise protein recognition to investigate protein–protein and protein–nucleic acid interactions. Dr. Tan serves as an Associate Editor for Frontiers in Molecular Biosciences: Molecular Recognition and is a member of the Editorial Board of Scientific Reports. His recent work has been published in leading journals\, including Journal of the American Chemical Society\, Nature Communications\, Theranostics\, Analytical Chemistry\, Chemical Communications.
URL:https://inside.wooster.edu/chemistry/event/chemistry-bcmb-seminar-2/
CATEGORIES:BCMB,Chemistry,Seminars,Seniors,STEM Success Initiative
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BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260917T110000
DTEND;TZID=America/New_York:20260917T130000
DTSTAMP:20261001T181125
CREATED:20260916T175757Z
LAST-MODIFIED:20260916T201827Z
UID:2560-1789642800-1789650000@inside.wooster.edu
SUMMARY:Chemistry & BCMB Summer Research/Internship Poster Session
DESCRIPTION:Location: Ruth W. Williams Hall of Life Sciences\, Room 140. \n\n\n\nCome learn about the research conducted over the summer by The College of Wooster’s Chemistry and BCMB majors. Donuts and cider will be provided.
URL:https://inside.wooster.edu/chemistry/event/chemistry-bcmb-summer-research-internship-poster-session/
CATEGORIES:BCMB,Chemistry,Seminars,Seniors
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260929T110000
DTEND;TZID=America/New_York:20260929T115000
DTSTAMP:20261001T181125
CREATED:20260916T180901Z
LAST-MODIFIED:20260924T133648Z
UID:2562-1790679600-1790682600@inside.wooster.edu
SUMMARY:Chemistry Seminar
DESCRIPTION:Dr. Paul Bonvallet\, Professor of Chemistry\, The College of Wooster\n\n\n\n\n\nFail Fast\, Fail Forward: Towards the Synthesis of Stackable Electron Donors\n\n\n\n Location: Ruth W. Williams Hall of Life Sciences\, Room 045. \n\n\n\nOrganic chemistry has a role to play in meeting the global demand for energy. Porphyrin-based electron donors\, which harvest light exceptionally well\, have potential as the next generation of materials in solar energy conversion. Individual pieces can self-assemble into a stacked “molecular ladder” through hydrogen bonding and other noncovalent interactions. The design is beautiful\, but the execution is… sometimes hard. Multi-step synthetic organic chemistry sometimes turns perfectly good ideas into challenges with solubility\, reactivity\, and fundamental design. These obstacles are common in research\, so progress depends not so much on the absence of failure but the ability to evaluate experiments quickly and to learn from every step along the way.
URL:https://inside.wooster.edu/chemistry/event/chemistry-seminar-6/
CATEGORIES:Chemistry,Seminars,STEM Success Initiative
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BEGIN:VEVENT
DTSTART;TZID=America/New_York:20261022T110000
DTEND;TZID=America/New_York:20261022T120000
DTSTAMP:20261001T181125
CREATED:20260916T194645Z
LAST-MODIFIED:20260916T201639Z
UID:2566-1792666800-1792670400@inside.wooster.edu
SUMMARY:Helen Murray Free Lecture - Technical
DESCRIPTION:Dr. Catherine Drennan\, Professor\, Departments of Biology and Chemistry\, Howard Hughs Medical Institute Investigator\, Massachusetts Institute of Technology \n\n\n\n\n\nRevealing the secrets of metalloenzymes one snapshot at a time\n\n\n\nLocation: Ruth W. Williams Hall of Life Sciences\, Room 060 \n\n\n\nAbstract:\n\n\n\n\n\n\n\nHow do microbes live on the pollutant carbon monoxide? How do microbes split the triple bond of nitrogen gas? When it comes to performing difficult chemistry\, microbes often combine a protein scaffold with a highly reactive metallocofactor; they essentially employ a “hired gun.” The Drennan lab combines X-ray crystallography and cryo-electron microscopy with other biophysical methods to reveal the secrets behind metalloenzyme chemistry. In this seminar\, Drennan will present her lab’s structural studies of ribonucleotide reductases (RNRs). RNRs use metallocofactors to generate radical species\, enabling the conversion of ribonucleotides (the building blocks of RNA) to deoxyribonucleotides (the building blocks of DNA). These enzymes are chemotherapeutic targets and proposed antibacterial targets. Here\, Drennan will describe how her lab has used biophysical methods to reveal RNR’s secrets.
URL:https://inside.wooster.edu/chemistry/event/helen-murray-free-lecture-technical/
CATEGORIES:BCMB,Chemistry,Neuroscience,Seminars,STEM Success Initiative
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20261022T190000
DTEND;TZID=America/New_York:20261022T200000
DTSTAMP:20261001T181125
CREATED:20260916T200857Z
LAST-MODIFIED:20260916T201553Z
UID:2569-1792695600-1792699200@inside.wooster.edu
SUMMARY:Helen Murray Free Lecture - Public
DESCRIPTION:Dr. Catherine Drennan\, Professor\, Department of Biology and Chemistry\, Howard Hughs Medical Institute Investigator\, Massachusetts Institute of Technology \n\n\n\n\n\nExploring the Molecular World\n\n\n\nLocation: Ruth W. Williams Hall of Life Sciences\, Room 060 \n\n\n\nThis talk is designed for and open to the general public. \n\n\n\nAbstract:\n\n\n\n\n\n\n\nProfessor Cathy Drennan of the Massachusetts Institute of Technology is fascinated by the molecular world. She wants to understand how protein molecules carry out the requisite work for cell survival. How do proteins transport cargo within a living cell? How do proteins break bonds into order to turn the building blocks of RNA into the building blocks of DNA? And importantly\, how can one watch a process that is too small to see? Research groups\, like the one that Drennan runs\, use biophysical methods to determine the three-dimensional structures of proteins at the atomic level. In this presentation\, Drennan will provide an overview of the methods that allow her to “see” the atoms that make-up protein molecules. She will tell you how she became an explorer of the molecular world. Her journey was not straightforward. In first grade\, she was diagnosed with dyslexia when she was not able to learn to read. By her second time through sixth grade\, she learned how to read by memorizing the shapes of words. Now she uses her shape-recognition abilities in her research to investigate the shapes of molecules. Drennan will share her journey and her research in a presentation designed for a general audience.
URL:https://inside.wooster.edu/chemistry/event/helen-murray-free-lecture-public/
CATEGORIES:BCMB,Chemistry,Seminars,STEM Success Initiative
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